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histone deacetylase 7 phosphate + H2O
histone deacetylase 7 + phosphate
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
P-MLC20 + H2O
MLC20 + phosphate
P-MLC20: phospho-peptide mimicking MLC20(3-26:P-Ser19)
-
-
?
phosphorylated glycogen synthase + H2O
glycogen synthase + phosphate
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
phosphorylated myosin + H2O
myosin + phosphate
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
phosphorylated phoshorylase B + H2O
phosphorylase B + phosphate
-
myosin-associated PP-1M
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
regulatory myosin light-chain phosphate + H2O
regulatory myosin light-chain + phosphate
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
[myosin regulatory light chain] phosphate + H2O
[myosin regulatory light chain] + phosphate
-
from chicken gizzard
-
-
?
additional information
?
-
histone deacetylase 7 phosphate + H2O
histone deacetylase 7 + phosphate
-
HDAC7, dephosphorylation induces reimport into the nucleus
-
-
?
histone deacetylase 7 phosphate + H2O
histone deacetylase 7 + phosphate
-
HDAC7, dephosphorylation induces reimport into the nucleus
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
isozyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
38 kDa catalytic subunit PP1c and holoenzyme are active, the 130 kDa subunit M130 activates PP1c activity, effect of truncation mutants of M130 on PP1c activity
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
from bovine stomach
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
role in the variable coupling between force and myosin light chain phosphorylation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
important role in regulating myofibroblast contraction, Rho/Rho kinase-mediated inhibition of MLCPPase is necessary for lysophosphatidic acid-promoted myofibroblast contraction, in contrast to smooth muscle cells, in which MLCPPase activity only regulates the sensitivity of the contractile response to Ca2+
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
holoenzyme and isolated catalytic subunit are active
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
SMP-I, -II, -III and -IV are active
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
38 kDa catalytic subunit PP1c and holoenzyme are active, the 130 kDa subunit M130 activates PP1c activity, effect of truncation mutants of M130 on PP1c activity
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
myosin regulatory light chain RLC from chicken gizzard, specificity of MLCP toward various phosphorylation sites of RCL, N-terminal region of RLC plays an important role in substrate recognition
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
reaction is a prerequisite for the actin activation of the myosin Mg2+-ATPase
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
myosin regulatory light chain RLC from chicken gizzard, specificity of MLCP toward various phosphorylation sites of RCL, N-terminal region of RLC plays an important role in substrate recognition
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
isozyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
isozyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
plays a critical regulatory role in the Ca2+ sensitivity of myosin phosphorylation and smooth muscle contraction
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
chicken gizzard 20 kDa myosin light-chain phosphate
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
from turkey gizzard
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
key smooth muscle regulatory protein, MLCP is required for muscle relaxation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
-
nonmuscle
-
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
-
nonmuscle
-
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
-
nonmuscle
-
-
?
phosphorylated glycogen synthase + H2O
glycogen synthase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
phosphorylated glycogen synthase + H2O
glycogen synthase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
a chymotryptic fragment of myosin, only SMP-III and SMP-IV are active, SMP-I and SMP-II not
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
from turkey gizzard
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-2A: low activity with native myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
from bovine stomach, P-myosin assembly is essential for SMMP activity
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
from turkey gizzard
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
catalytic subunit is active, holoenzyme not
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
myosin heavy chain plays a role in the smooth muscle MLCP-myosin regulatory light chain interaction, specificity toward myosin phosphorylated at various sites of the myosin regulatory light chain RLC, role of the N-terminal region of RLC in the dephosphorylation of myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
only SMP-III and SMP-IV are active, SMP-I and SMP-II not
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
from turkey gizzard
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
myosin heavy chain plays a role in the smooth muscle MLCP-myosin regulatory light chain interaction, specificity toward myosin phosphorylated at various sites of the myosin regulatory light chain RLC, role of the N-terminal region of RLC in the dephosphorylation of myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1M is more active towards native myosin than PP-1G
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-2A: low activity with native myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
from turkey gizzard
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
-
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
-
holoenzyme and isolated catalytic subunit are active, phosphorylated at 2 sites, in absence of bound calmodulin rapid dephosphorylation at both sites, in presence of bound calmodulin dephosphorylation of only one site
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
-
autophosphorylated myosin light chain kinase is a good substrate for the kinase- and myosin-associated protein phosphatase KAMPPase
-
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
-
SMP-I modulates the activity of myosin-light chain kinase
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
-
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
38 kDa catalytic subunit PP1c
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chains and phosphorylase A at comparable rates
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
radixin + H2O
?
-
-
-
-
?
radixin + H2O
?
-
an ERM protein
-
-
?
regulatory myosin light-chain phosphate + H2O
regulatory myosin light-chain + phosphate
-
-
-
-
?
regulatory myosin light-chain phosphate + H2O
regulatory myosin light-chain + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
substrate is phosphorylated Physarum myosin II
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
substrate is regulatory light chain (LC20) of myosin II, MLCP-mediated dephosphorylation of LC20 at Ser19
-
-
?
additional information
?
-
-
both gene products of protein phosphatase 1, PP1, (catalytic subunit of the myosin phosphatase) ppp1cba and ppp1cbb interact with Mypt1 (regulatory subunit of the myosin phosphatase) and assemble an active myosin phosphatase complex
-
-
?
additional information
?
-
-
enzyme binds to vesicles of acidic phospholipids, i.e. phosphatidylserine, phosphatidylinositol and phosphatidic acid, but not to neutral phospholipids, phosphatidylserine binding decreases by increasing ionic strength and Mg2+ concentration, phospholipid binding is associated with the C-terminal part of the 130/133 kDa myosin-binding subunit and the 20 kDa regulatory subunit
-
-
?
additional information
?
-
-
130 kDa subunit MLCPa: elongated structure with 3 globular domains connected by flexible strands
-
-
?
additional information
?
-
-
interactions among the 38 kDa catalytic subunit PP1c, the 130 kDa and the 20 kDa non-catalytic subunits M130 and M20 or fragments of them, M130 has 2 binding sites for PP1c: one site in the N-terminal 38 residues and a weaker site in the ankyrin repeats region, activation of phosphatase and binding of PP1c and substrate are properties of the N-terminal one-third of M130
-
-
?
additional information
?
-
-
involved in force regulation in smooth muscle, the relative expression of splice-in/splice-out myosin-targeting subunit isoforms determines the magnitude of agonist-induced force enhancement/Ca2+ sensitization
-
-
?
additional information
?
-
-
130 kDa subunit MLCPa: elongated structure with 3 globular domains connected by flexible strands
-
-
?
additional information
?
-
role of the heart-specific small regulatory subunit hHS-M21 of MLCP
-
-
?
additional information
?
-
-
thrombin activates the Rho/Rho kinase pathway to inactivate myosin light chain phosphatase as part of a signaling network that controls myosin light chain phosphorylation and contraction in endothelial cells
-
-
?
additional information
?
-
-
plays a key role in platelet function
-
-
?
additional information
?
-
-
myosin phosphatase subunits protein phosphatase 1beta (PP1beta) and myosin phosphatase targeting subunit (Mypt1) interact with transcription factor Nkx2.5 and inhibit its transcriptional activity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
KAMPPase: kinase- and myosin-associated protein phosphatase, functional multienzyme complex composed of a myofibrillar form of smooth muscle myosin light chain phosphatase and myosin light chain kinase with or without calmodulin, regulation of the phosphatase activity
-
-
?
additional information
?
-
-
two forms of SMP-I, the intact form and the catalytic subunit, may act in an opposite manner to regulate smooth muscle contraction in vivo
-
-
?
additional information
?
-
-
together with myosin light chain kinase key regulatory enzyme of smooth muscle
-
-
?
additional information
?
-
-
regulation of the MLCP activity
-
-
?
additional information
?
-
-
involved in the regulation of smooth muscle contraction, regulation of the MLCP activity
-
-
?
additional information
?
-
-
pulmonary hypertension down-regulates pulmonary vascular MLCP expression, the maintenance of a high pulmonary vascular resistance may be secondary to abnormalities in tissue content and/or activity of MLCP
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
?
additional information
?
-
-
insulin stimulates the binding of MRIP (myosin phosphatase Rho-interacting protein) to MYPT1 in a dose- and time-dependent manner, as determined by immunoprecipitation
-
-
?
additional information
?
-
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
?
additional information
?
-
-
regulation mechanism of MLCP activity
-
-
?
additional information
?
-
-
involved in smooth muscle relaxation
-
-
?
additional information
?
-
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
?
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metabolism
-
phosphorylation of MYPT1 is a major mechanism of MLCP regulation, but protein-protein interactions may also be important. Ca2+-dependent and Rho-associated kinase-mediated regulation of myosin light chain kinase and myosin light chain phosphatase, respectively, in the arterial myogenic response, molecular mechanisms, overview
malfunction
-
a loss-of-function mutation of flapwing, which encodes the catalytic subunit of protein phosphatase 1beta, disrupts oocyte polarization. Proliferation and differentiation of the posterior follicle cells are affected by FP41, also FP41 mutation disrupts cell differentiation and Notch signaling of the cells. Excessive myosin activity in the posterior follicle cells causes oocyte mispolarization and defective Notch signaling and endocytosis in the posterior follicle cells, phenotype, detailed overview. The Notch intracellular domain can rescue the Notch signaling phenotype, but not the oocyte polarity phenotype of flwFP41 mutant cells
malfunction
-
enzyme domain MYPT mutation, MEL-11, causes cytokinesis failure
malfunction
deletion of MYPT1 in vascular smooth muscle enhances RLC (myosin regulatory light chain) phosphorylation and contractile activity, which may contribute to the development of hypertension in vivo
malfunction
knockdown of MYPT1 does not cause apoptosis in normal HeLa cells but the percentage of TNF/CHX-induced apoptotic cells is increased in MYPT1-depleted cells
malfunction
-
Morpholino knock-down of ppp1cba and ppp1cbb results in severe defects in morphogenetic cell movements during gastrulation through loss of myosin phosphatase function
physiological function
-
MLCP is directly and critically involved in endothelial cell barrier regulation, enhancement, and protection, with involvement of catalytic enzyme subunit CS1beta in the endothelial cell barrier enhancement induced by extracellular purines
physiological function
-
myosin phosphatase is required for contractile ring disassembly at the end of cytokinesis, it is involved in the assembly of ring canals derived from incomplete cytokinesis and function as intracellular bridges between nurse cells, thereby allowing cytoplasmic flow from nurse cells to oocytes. Myosin phosphatase must be temporally controlled during cytokinesis: it is first inactivated for the activation of a contractile ring at the initial stage of cytokinesis and then inactivated for the disassembly of the contractile ring
physiological function
-
physiological roles of myosin light chain kinase, MLCK, activation and myosin light chain phosphatase, MLCP, inhibition in the myogenic response, MLCP inhibition may also be required to slow the rate of LC20 dephosphorylation, mechanism, overview
physiological function
-
PP1beta, by regulating myosin activity, controls the generation of the oocyte polarizing signal, it is essential for dephosphorylation and inactivation of the non-muscle myosin II light chain encoded by spaghetti squash. PP1beta regulates the membrane levels of apical complexes in the posterior follicle cells
physiological function
-
the heart-specific small subunit, hHS-M21, is a heart-specific effector of Rho-associated kinase and plays a regulatory role in the MYPT1 phosphorylation at Thr-696 by Rho-associated kinase, molecular mechanism, overview
physiological function
-
Par-1 (cell polarity protein) binds to myosin phosphatase and phosphorylates it at a known inactivating site. Par-1 thus promotes phosphorylated myosin regulatory light chain, thereby increasing Myo-II activity
physiological function
as motor axons exit from the spinal cord and extend through extracellular matrix produced by adjacent notochord cells,these cells shift several cell diameters caudally. Individual motoneuron cell bodies stay aligned with their extending axons. This alignment requires myosin phosphatase activity within motoneurons, and mutations in the myosin phosphatase subunit Mypt1 increase myosin phosphorylation causing a displacement between motoneuron cell bodies and their axons
physiological function
-
differences in MYPT1 exon 24 isoforms, endothelial nitric oxide synthase eNOS, and potassium ion channel Kir2.1 distinguish epicardial arteries and resistance coronary arterioles. MYPT1 isoforms are distinct in the epicardial arteries (exon 24 -/leucine zipper +) and resistance arterioles (exon 24 +/leucine zipper -) and unchanged by exercise training or coronary occlusion. MYPT1, CPI-17 and PDE5 mRNA levels are not different between arteries and arterioles while Kir2.1 and eNOS are 6.6fold and 3.9fold higher in the arterioles
physiological function
interaction of myosin phosphatase target subunit (MYPT1) and myosin phosphatase-RhoA interacting protein (MRIP) causes colocalization of myosin phosphatase and RhoA to actomyosin. The residues 724-837 of MRIP are sufficient for the MYPT1/MRIP interaction. MRIP binds to MYPT1 as either a monomer or a dimer. The leucine repeat region of MYPT1, LR (residues 991-1030) is sufficient to account for the MYPT1/MRIP interaction. Point mutations that replace glutamic acids 998-1000 within LR reduce the binding affinity toward MRIP
physiological function
-
myosin light-chain phosphatase subunit flapwing (flw) is a key regulator of basal myosin oscillations and cell contractions underlying egg chamber elongation. Flw expression decreases specifically on the basal side of follicle cells at the onset of contraction and flw controls the initiation and periodicity of basal actomyosin oscillations
physiological function
phosphorylation of MYPT1 residue T694, but not T852, is a primary mechanism contributing to inhibition of myosin light chain phosphatase activity and enhancement of myosin regulatory light chain phosphorylation in vivo. Smooth muscles containing the T694A mutation show a significant reduction of force along with reduced myosin regulatory light chain phosphorylation. The contractile responses of the T694A mutant smooth muscle are independent of RhoA-associated protein kinase ROCK activation
physiological function
Rho family G-proteinRac1 inhibits the activity of myosin light chain phosphatase MLCP through a phosphatase that targets MYPT1 and specific inhibitor CPI-17 rather than through the RhoA-Rho dependent kinase (ROCK) pathway. Rac1 inhibition decreases agonist-induced increase in myosin light chain phosphorylation
physiological function
silencing of, the regulatory subunit of myosin phosphatase MYPT1 has a negative impact on the migration of keratinocytes during wound closure and it influences the cell-cell adhesion properties by decreasing the impedance of HaCaT cells. Myosin phosphatase contributes to the mediation of wound healing by regulating the Akt signaling pathway
physiological function
silencing of, the regulatory subunit of myosin phosphatase MYPT1 has a negative impact on the migration of keratinocytes during wound closure and it influences the cell-cell adhesion properties by decreasing the impedance of HaCaT cells. Myosin phosphatase contributes to the mediation of wound healing by regulating the Akt signaling pathway
physiological function
-
transgenic mice with cardiac-specific overexpression of heart-specific small subunit of myosin light chain phosphatase hHS-M21 show increased Ca2+ sensitivity of cardiac muscle contraction in vivo, which is not followed by an increased phosphorylation of myosin light chain 2 isoforms. hHS-M21 transgenic mice developed severe systolic dysfunction with myocardial fibrosis and degeneration of cardiomyocytes in association with sinus bradycardia and atrioventricular conduction defect. The contractile dysfunction and cardiac fibrosis are improved by treatment with the Rho kinase inhibitor fasudil
physiological function
-
treatment of Triton-skinned rat caudal arterial smooth muscle strips with the membrane-impermeant phosphatase inhibitor microcystin or treatment of intact tissue with the membrane-permeant phosphatase inhibitor calyculin A induces slow, sustained contractions that correlate with phosphorylation of MYPT1 at 7 to more than 10 sites
physiological function
variants of myosin light chain phosphatase regulatory subunit Mypt1 are generated by alternative splicing of the 31 nt exon 24, i.e. E24. In mice that underwent Tamoxifen-inducible and smooth muscle-specific knockout of E24 after weaning, deletion of a single allele of E24 enhances vasorelaxation of first-order mesenteric arteries to diethylamine-NONOate and to cGMP in permeabilized and calcium-clamped arteries and lowers blood pressure. First-order mesenteric arteries from homozygous E24 knockout mice show reduced force generation to alpha-adrenergic activation. 2 weeks of high-salt diet increase mesenteric arteries force generation to phenylephrine in control mice, which is markedly suppressed in the E24 knockout homozygotes
additional information
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myosin II association with actin, which triggers contraction, is regulated by orchestrated waves of phosphorylation/dephosphorylation of the myosin regulatory light chain. Dephosphorylation is mediated by myosin phosphatase
additional information
-
myosin light chain phosphatase is regulated by phosphorylation of the catalytic subunit, the heart-specific small subunit, hHS-M21, plays a role in the regulation by phosphorylation, molecular mechanism, overview. Two isoforms of hHSM21, hHS-M21Aand hHS-M21B, preferentially bound the C-terminal one-third region of MYPT1 and MYPT2, respectively. Amino acid substitutions at a phosphorylation site of MYPT1, Ser852, impaired the binding of MYPT1 and hHS-M21. The hHS-M21 increases the phosphorylation level of MYPT1 at Thr696, which is attenuated by Rho-associated kinase, ROCK, inhibitors and small interfering RNAs for Rho-associated kinase
additional information
-
regulation of the enzyme involving ERM proteins ezrin, radixin, moesin, and isozymes of myosin PPase targeting subunit 1, MYPT1, overview
additional information
-
smooth muscle myosin light chain phosphatase, MLCP, consists of three proteins, the catalytic PP1c-delta phosphatase, the MYPT1 targeting subunit, and M20 protein. Binding of PP1c-delta to MYPT1 occurs via a RVXF motif immediately adjacent to a series of ankyrin repeats that are implicated in protein-protein interactions. Myosin binding may occur over a region at the C-terminus that contains one of the two major ROK phosphorylation sites, T697 and T855. MYPT1 is a substrate for phosphorylation by several serine/threonine kinases that modulate MLCP activity and/or alter myosin binding. MYPT1 has three essential functions: (i) to confer myosin substrate specificity to the complex, (ii) to enhance the specific activity of PP1c-delta in dephosphorylating phospho-LC20, and (iii) to provide a means by which MLCP activity can be regulated by a variety of stimuli
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2012
Homo sapiens
brenda
Lee, J.H.; Palaia, T.; Ragolia, L.
Impaired insulin-stimulated myosin phosphatase Rho-interacting protein signaling in diabetic Goto-Kakizaki vascular smooth muscle cells
Am. J. Physiol. Cell Physiol.
302
C1371-C1381
2012
Rattus norvegicus
brenda
Khasnis, M.; Nakatomi, A.; Gumpper, K.; Eto, M.
Reconstituted human myosin light chain phosphatase reveals distinct roles of two inhibitory phosphorylation sites of the regulatory subunit, MYPT1
Biochemistry
53
2701-2709
2014
Homo sapiens (O14974), Homo sapiens
brenda
Ryan, T.; Shelton, M.; Lambert, J.P.; Malecova, B.; Boisvenue, S.; Ruel, M.; Figeys, D.; Puri, P.L.; Skerjanc, I.S.
Myosin phosphatase modulates the cardiac cell fate by regulating the subcellular localization of Nkx2.5 in a Wnt/Rho-associated protein kinase-dependent pathway
Circ. Res.
112
257-266
2013
Homo sapiens
brenda
Majumder, P.; Aranjuez, G.; Amick, J.; McDonald, J.A.
Par-1 controls myosin-II activity through myosin phosphatase to regulate border cell migration
Curr. Biol.
22
363-372
2012
Drosophila melanogaster
brenda
Qiao, Y.N.; He, W.Q.; Chen, C.P.; Zhang, C.H.; Zhao, W.; Wang, P.; Zhang, L.; Wu, Y.Z.; Yang, X.; Peng, Y.J.; Gao, J.M.; Kamm, K.E.; Stull, J.T.; Zhu, M.S.
Myosin phosphatase target subunit 1 (MYPT1) regulates the contraction and relaxation of vascular smooth muscle and maintains blood pressure
J. Biol. Chem.
289
22512-22523
2014
Mus musculus (Q9DBR7)
brenda
Iwasaki, T.; Katayama, T.; Kohama, K.; Endo, Y.; Sawasaki, T.
Myosin phosphatase is inactivated by caspase-3 cleavage and phosphorylation of myosin phosphatase targeting subunit 1 during apoptosis
Mol. Biol. Cell
24
748-756
2013
Homo sapiens (O14974), Mus musculus (Q9DBR7)
brenda
Jayashankar, V.; Nguyen, M.J.; Carr, B.W.; Zheng, D.C.; Rosales, J.B.; Rosales, J.B.; Weiser, D.C.
Protein phosphatase 1 beta paralogs encode the zebrafish myosin phosphatase catalytic subunit
PLoS ONE
8
e75766
2013
Danio rerio
brenda
Sutherland, C.; MacDonald, J.A.; Walsh, M.P.
Analysis of phosphorylation of the myosin-targeting subunit of myosin light chain phosphatase by Phos-tag SDS-PAGE
Am. J. Physiol. Cell Physiol.
310
C681-C691
2016
Rattus norvegicus, Gallus gallus (Q90623)
brenda
Reho, J.J.; Kenchegowda, D.; Asico, L.D.; Fisher, S.A.
A splice variant of the myosin phosphatase regulatory subunit tunes arterial reactivity and suppresses response to salt loading
Am. J. Physiol. Heart Circ. Physiol.
310
H1715-H1724
2016
Mus musculus (Q9DBR7)
brenda
Arimura, T.; Muchir, A.; Kuwahara, M.; Morimoto, S.; Ishikawa, T.; Du, C.K.; Zhan, D.Y.; Nakao, S.; Machida, N.; Tanaka, R.; Yamane, Y.; Hayashi, T.; Kimura, A.
Overexpression of heart-specific small subunit of myosin light chain phosphatase results in heart failure and conduction disturbance
Am. J. Physiol. Heart Circ. Physiol.
314
H1192-H1202
2018
Mus musculus
brenda
Horvath, D.; Sipos, A.; Major, E.; Konya, Z.; Batori, R.; Dedinszki, D.; Szoell Si, A.; Tamas, I.; Ivan, J.; Kiss, A.; Erd di, F.; Lontay, B.
Myosin phosphatase accelerates cutaneous wound healing by regulating migration and differentiation of epidermal keratinocytes via Akt signaling pathway in human and murine skin
Biochim. Biophys. Acta
1864
3268-3280
2018
Homo sapiens (O14974), Homo sapiens, Mus musculus (Q9DBR7), Mus musculus
brenda
Shibata, K.; Sakai, H.; Huang, Q.; Kamata, H.; Chiba, Y.; Misawa, M.; Ikebe, R.; Ikebe, M.
Rac1 regulates myosin II phosphorylation through regulation of myosin light chain phosphatase
J. Cell. Physiol.
230
1352-1364
2015
Rattus norvegicus (Q10728)
brenda
Chen, C.; Chen, X.; Qiao, Y.; Wang, P.; He, W.; Zhang, C.; Zhao, W.; Gao, Y.; Chen, C.; Tao, T.; Sun, J.; Wang, Y.; Gao, N.; Kamm, K.; Stull, J.; Zhu, M.
In vivo roles for myosin phosphatase targeting subunit-1 phosphorylation sites T694 and T852 in bladder smooth muscle contraction
J. Physiol.
593
681-700
2015
Mus musculus (Q9DBR7), Mus musculus
brenda
Zheng, X.; Heaps, C.; Fisher, S.
Myosin phosphatase isoforms and related transcripts in the pig coronary circulation and effects of exercise and chronic occlusion
Microvasc. Res.
98
166-171
2015
Sus scrofa
brenda
Valencia-Exposito, A.; Grosheva, I.; Miguez, D.G.; Gonzalez-Reyes, A.; Martin-Bermudo, M.D.
Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
Nat. Commun.
7
10746
2016
Drosophila melanogaster
brenda
Bremer, J.; Granato, M.
Myosin phosphatase fine-tunes zebrafish motoneuron position during axonogenesis
PLoS Genet.
12
e1006440
2016
Danio rerio (Z4YIS0)
-
brenda
Lee, E.; Stafford, W.3.
Interaction of myosin phosphatase target subunit (MYPT1) with myosin phosphatase-RhoA interacting protein (MRIP) a role of glutamic acids in the interaction
PLoS One
10
e0139875
2015
Homo sapiens (O14974)
brenda
Lartey, J.; Taggart, J.; Robson, S.; Taggart, M.
Altered expression of human smooth muscle myosin phosphatase targeting (MYPT) isovariants with pregnancy and labor
PLoS ONE
11
e0164352
2016
Homo sapiens (O14974), Homo sapiens
brenda