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Information on EC 2.7.11.18 - myosin-light-chain kinase and Organism(s) Mus musculus and UniProt Accession Q3UIZ8
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2.7.11.18 myosin-light-chain kinaseIUBMB Comments
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.
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Word Map
- 2.7.11.18
-
contractile
- actin
- junction
- artery
- rho
- pkc
- agonist
- gizzard
- cytoskeletal
- actomyosin
-
tension
- occludin
-
rock
-
calmodulin-binding
-
actin-activated
-
isometric
-
rho-associated
- mlc20
-
paracellular
-
ca2+-independent
-
actin-myosin
-
rho-kinase
- wortmannin
-
zonula
- mypt1
-
cam-binding
-
actin-binding
-
cam-dependent
- trifluoperazine
- caldesmon
-
myofilament
-
hyperpermeability
-
thrombin-induced
-
thiophosphorylation
- mg2+-atpase
- calyculin
-
pseudosubstrate
- blebbistatin
- idella
-
diphosphorylation
- calponin
-
cross-bridge
- meromyosin
- medicine
-
mgatpase
-
myosin-binding
-
monoxime
-
n-6-aminohexyl-5-chloro-1-naphthalenesulfonamide
-
calmodulin-activated
-
superprecipitation
- cak
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mlck, myosin light chain kinase, myosin light-chain kinase, mlc kinase, smooth muscle myosin light chain kinase, smmlck, nmmlck, myosin kinase, cmlck, skmlck, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
calcium/calmodulin-dependent myosin light chain kinase
-
-
-
-
kinase, myosin light-chain (phosphorylating)
-
-
-
-
MLCK
myosin kinase
-
-
-
-
myosin light chain kinase
myosin light chain protein kinase
-
-
-
-
myosin light-chain kinase
smooth-muscle-myosin-light-chain kinase
-
-
-
-
MLCK
-
-
myosin light chain kinase
-
-
myosin light-chain kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[myosin light chain] O-phosphotransferase
Requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY
51845-53-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + myosin regulatory light chain
ADP + myosin regulatory light chain phosphate
-
-
-
-
?
ATP + myosin regulatory light chain
ADP + phosphorylated myosin regulatory light chain
-
-
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
MLC2
-
-
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
-
-
-
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
MLCK plays a key role in the control of MLC-phosphorylation status, and it modulates barrier function through its regulation of intracellular contractile machinery, overview, endothelial mechanism of MLC-dependent barrier injury in burns, overview
-
-
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
myosin II activation is essential for stress fiber and focal adhesion formation, and is implicated in integrin-mediated signaling events
-
-
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
-
-
-
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
-
-
?
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, in aortic rings from mice in which alpha1, the major catalytic subunit isoform in arterial smooth muscle, is deleted, KCl- or phenylephrine-induced contraction is increased, overview
-
-
?
ATP + myosin light chain 2
ADP + myosin light chain 2 phosphate
MLCK is involved in sarcomere organization, cardiac MLCK promotes sarcomere organization and increases cardiomyocyte contractility, overview
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
-
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
non-muscle myosin II and preferred substrate smooth muscle myosin II
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
phosphorylation of Thr-18/Ser-19 on the regulatory light chain of myosin II
-
-
?
additional information
?
-
-
the enzyme is involved, probably via microfilament assembly, in sperm chromatin-induced cortical reorganization during oocyte maturation to a polarized egg
-
-
?
additional information
?
-
-
inhibition of the enzyme retards the growth of mammary cancer cells
-
-
?
additional information
?
-
-
regulation of the MLCK promoters and gene expression involving myocardin, model, overview
-
-
?
additional information
?
-
-
the myosin light chain kinase plays a role in the regulation of epithelial cell survival, and in the generation of pro-survival signals in both untransformed and transformed epithelial cells, apoptosis following inhibition of myosin II activation by MLCK is probably meditated through the death receptor pathway, overview
-
-
?
additional information
?
-
-
MLCK is a substrate of AMP-activated protein kinase, AMPK
-
-
?
additional information
?
-
-
myosin light chain kinase is central to smooth muscle contraction and required for gastrointestinal motility in mice, overview
-
-
?
additional information
?
-
the cardiac-specific isozyme probably performs also autophosphorylation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + myosin light chain
ADP + phosphorylated myosin light chain
-
activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction, in aortic rings from mice in which alpha1, the major catalytic subunit isoform in arterial smooth muscle, is deleted, KCl- or phenylephrine-induced contraction is increased, overview
-
-
?
ATP + myosin light chain 2
ADP + myosin light chain 2 phosphate
MLCK is involved in sarcomere organization, cardiac MLCK promotes sarcomere organization and increases cardiomyocyte contractility, overview
-
-
?
ATP + myosin regulatory light chain
ADP + phosphorylated myosin regulatory light chain
-
-
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice
-
-
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
MLCK plays a key role in the control of MLC-phosphorylation status, and it modulates barrier function through its regulation of intracellular contractile machinery, overview, endothelial mechanism of MLC-dependent barrier injury in burns, overview
-
-
?
ATP + light chain myosin II
ADP + phosphorylated light chain myosin II
-
myosin II activation is essential for stress fiber and focal adhesion formation, and is implicated in integrin-mediated signaling events
-
-
?
ATP + myosin light chain
ADP + myosin light chain phosphate
-
the MLCK family plays an essential role in regulation of actin/myosin organization, sarcomere assembly and cytoskeletal dynamics
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
-
-
-
-
?
ATP + [myosin light chain]
ADP + [myosin light chain] phosphate
non-muscle myosin II and preferred substrate smooth muscle myosin II
-
-
?
additional information
?
-
-
the enzyme is involved, probably via microfilament assembly, in sperm chromatin-induced cortical reorganization during oocyte maturation to a polarized egg
-
-
?
additional information
?
-
-
inhibition of the enzyme retards the growth of mammary cancer cells
-
-
?
additional information
?
-
-
regulation of the MLCK promoters and gene expression involving myocardin, model, overview
-
-
?
additional information
?
-
-
the myosin light chain kinase plays a role in the regulation of epithelial cell survival, and in the generation of pro-survival signals in both untransformed and transformed epithelial cells, apoptosis following inhibition of myosin II activation by MLCK is probably meditated through the death receptor pathway, overview
-
-
?
additional information
?
-
-
MLCK is a substrate of AMP-activated protein kinase, AMPK
-
-
?
additional information
?
-
-
myosin light chain kinase is central to smooth muscle contraction and required for gastrointestinal motility in mice, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
Mg2+
Ca2+
-
the enzyme is dependent on Ca2+ and calmodulin, the intracellular Ca2+ concentration has regulatory effect, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(5-Iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine hydrochloride
-
-
-
11-(3-chloro-6-iminopyridazin-1(6H)-yl)-N-(6-phenylpyridazin-3-yl)undecanamide
-
highly specific inhibitor, competitive to ATP binding
Carbachol
-
increases Ca2+ concentration, MLCK activation and regulatory light chain phosphorylation
KCl
-
increases Ca2+ concentration, MLCK activation and regulatory light chain phosphorylation
Peptide 18
-
i.e. H-RKKYKYRRK-NH2, specifically inhibits the enzyme and prevents sperm chromatin-induced cortical reorganization in eggs in vivo
-
ML-7
-
specifically inhibits the enzyme and prevents sperm chromatin-induced cortical reorganization in eggs in vivo
ML-7
-
inhibition of MLCK induces apoptosis in adherent cells and disrupts cell-cell adhesion
ML-7
-
specific inhibitor of MLCK, has a chemopreventive effect in an in vitro mouse mammary organ culture model, in vivo the inhibitor retards the growth of mammary tumours, acts as an adjuvant to etoposide stimulating its ability to prevent growth of established tomours, overview
ML-9
-
inhibition of MLCK induces apoptosis in adherent cells and disrupts cell-cell adhesion
ML-9
-
i.e. 1-(5-chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine, inhibits MLCK and paracellular permeability increases in several intestinal epithelial models
additional information
-
inhibitor effects on enzyme activity in intestinal tissues, overview
-
additional information
-
PAK phosphorylation of MLCK by p21-activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calyculin A
calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N
additional information
-
the enzyme is activated by phosphorylation through mitogen activated protein kinase MAPK
-
additional information
-
myocardin, a cardiac SAP, SAF-A/B, acinus, PIAS, domain-containing protein, is important in regulation of enzyme expression, overview, induction of enzyme expression by the thyrotroph embryonic factor binding to the the CArG box of the promoter, TEF
-
additional information
-
activation of the RhoA pathway can inhibit myosin phosphatase activity, thereby enhancing the effects of the kinase-mediated phosphorylation of myosin light chain
-
additional information
-
treatment with pentoxifylline attenuates activation of MLCK likely through its ability to decrease local tumor necrosis factor-alpha synthesis and nucleat factor kappaB activation after burn
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of obscurin-MLCK-like kinase is restricted to muscles in the myonucleus
-
the long isoform of MLCK, MLCK-210, is the predominant isoform expressed in vascular endothelial cells
additional information
additional information
-
two isozymes: the endothelial, long or nonmuscle 220-kDa MLCK and a short, smooth muscle 130-kDa MLCK, mechanism of regulation of tissue-specific mylk gene expression, overview
additional information
-
developmental pattern of obscurin and obscurin-associated kinase expression, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
MAPK3/1 (ERK1/2, EC 2.7.11.24) and myosin light chain kinase in mammalian eggs affect myosin-II function and regulate the metaphase II state in a calcium- and zinc-dependent manner. Vertebrate eggs are arrested at metaphase of meiosis II, a state classically known as cytostatic factor arrest. Maintenance of this arrest until the time of fertilization and then fertilizationinduced exit from metaphase II are crucial for reproductive success, overview
physiological function
malfunction
physiological function
malfunction
in cultured cardiomyocytes, the knockdown of cMLCK impaired epinephrine-induced activation of sarcomere reassemble and overexpression of cMLCK promoted sarcomere organization. The lack of MLC2 phosphorylation in heart induces reduction in cardiac performance in genetically modified cMLCK knockout mice. Reduced levels of MLC2 phosphorylation induces cardiac dysfunction
malfunction
in meiosis I, MLCK inhibition and other myosin perturbations impair spindle migration and first polar body emission. Inhibition of the MEK1/2-MAPK pathway with U0126 leads to reduced levels of phosphorylated myosin-regulatory light chain (pMRLC) and causes a reduction in cortical tension, effects that are mimicked by treatment with the myosin light chain kinase (MLCK) inhibitor ML-7. MAPK or MLCK inhibition induces loss of normal cortical spindle localization or parthenogenetic egg activation. This parthenogenesis is dependent on cytosolic and extracellular calcium and can be rescued by hyperloading eggs with zinc, suggesting that these effects of inhibition of MLCK or the MAPK pathway are linked with dysregulation of ion homeostasis, overview
physiological function
in cardiac muscle the dominant regulatory mechanism is centered on the thin-filament protein, troponin, where binding of Ca2+ to troponin C induces contraction. MLC2 phosphorylation plays modulatory roles. The spatial gradient of MLC2 phosphorylation from base to apex and from endocardium to epicardium plays a physiological role in producing cardiac torsion and maintaining normal cardiac contraction. MLC2 phosphorylation may influence actin-myosin interactions independent to the actin-bound regulatory proteins. Cardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. The papillary muscle twitch tension induced by electrical field stimulation is smaller in C57BL/6N than C57BL/6J. Phenylephrine has no effect on MLC2v phosphorylation in either strains but increased the twitch tension more potently in C57BL/6J than in C57BL/6N. Calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N. cMLCK is an indispensable kinase for MLC2 phosphorylation in myocardium
physiological function
MLCK phosphorylates myosin regulatory light chain (MRLC, also known as MYL9), which enables myosin-II organization into bipolar thick filaments
malfunction
-
MLCK-deficient mice lack bronchial constrictions in normal and asthmatic airways, while the asthmatic inflammation response is not affected
malfunction
MLCK activates myosin Mg-ATPase activity by phosphorylating Thr-18/Ser-19 on the RLC of myosin II, thereby initiating cross-bridge movements of both smooth muscle and non-muscle. MLCK deletion causes enhanced cell protrusion along with a reduction of membrane tension and is rescued by kinase-dead MLCK or five-DFRXXL motif. The deletion of MLCK results in fast cell migration, enhanced protrusion formation, but no alteration of myosin light chain phosphorylation. The mutant cells show reduced membrane tether force and fewer membrane F-actin filaments, as well as a higher average migrating velocity and protrusion compared to wild-type
malfunction
-
mice harboring a deletion of the nmMLCK gene exhibit protection from radiation-induced lung injury, as assessed by attenuated vascular leakage and leukocyte infiltration
physiological function
-
myosin light chain kinase acts as a central participant in the contractile signaling module of tonic smooth muscle
physiological function
-
phosphorylation of myosin light chains by myosin light chain kinase activates endothelial contractile elements and results in a rearrangement of the cytoskeleton
physiological function
MLCK regulates cell migration not by myosin regulatory light chain phosphorylation but possibly through a membrane tension-based mechanism, which is a distinct regulatory mechanism of protrusion during cell migration. MLCK is not required for myosin phosphorylation in a migrating cell, but negatively controls migration by maintaining membrane tension. A critical role of MLCK in cell migration involves regulating the cell membrane tension and protrusion necessary for migration, thereby stabilizing the membrane skeleton through F-actin-binding activity. MLCK regulates the membrane F-actin skeleton. MLCK regulates cell spreading through 5DFRXXL in a kinase-independent manner
physiological function
-
lamellipodia contractility regulated by the enzyme is responsible for the intriguing turning behavior of T cells climbing sharp-edged ramp-like structures. The enzyme activity is responsible for the reduction of velocity and turning of T cells encountering ramp-like structures
physiological function
-
the nonmuscle myosin light chain kinase plays a key role in vascular barrier regulation in radiation-induced lung injury
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MYLK3_MOUSE
795
0
86372
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the endothelial isozyme possesses a catalytic domain including the actin-binding domain and the calmodulin binding domain, like the smooth muscle isozyme, but also a protein-protein interaction domain including SH2 and SH3 domains
additional information
the MLCK locus encodes three transcripts from alternative promoters and produces two MLCK isoforms (short MLCK and long MLCK) and a C-terminal Ig module (telokin). Long MLCK (L-MLCK) is identical to short MLCK (S-MLCK) apart from a unique N-terminal extension containing two extra DFRXXL motifs and six Ig modules
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
the enzyme is phosphorylated and activated by mitogen activated protein kinase MAPK
phosphoprotein
-
PAK phosphorylation of MLCK by p21- activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity
phosphoprotein
the cardiac-specific isozyme probably performs also autophosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T146A
a naturally occuring point mutation in strain C57BL/6N, the mutation locates in exon1 of gene Mylk3
additional information
additional information
-
construction of eMLCK or smMLCK knockout mutant mice by genetic or chemical methods, overview
additional information
-
long isozyme MLCK-210-deficient mice display a significantly improved survival with a greatly attenuated microvascular hyperpermeability response to albumin and fluid
additional information
-
generation of tamoxifen-inducible and smooth muscle-specific MLCK knockout mutant mice with loss of function and impaired smooth muscle contraction, severe gut dysmotility, phenotype, overview
additional information
generation of enzyme MLCK deletion in intestinal smooth muscle cells, phenotype, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Mylk3, two isoforms X1 and isoform X2, DNA and amino acid sequence determination and analysis, sequence comparions
DNA and amino acid sequence determination and analysis, expression analysis in cardiac smooth muscle, overview, expression of HA-tagged MLCK
expression of wild-type and dominant-negative MLCK in untransformed and Ras-transformed MCF-10A cells
-
gene Mlck, expression analysis, transgenic expression in mice bladder smooth muscle via adenoviral transfection
-
gene Mylk, the MLCK locus encodes three transcripts from alternative promoters and produces two MLCK isoforms (short MLCK and long MLCK) and a C-terminal Ig module (telokin). Long MLCK (L-MLCK) is identical to short MLCK (S-MLCK) apart from a unique N-terminal extension containing two extra DFRXXL motifs and six Ig modules
gene mylk1, located on chromosome 16, contains at least 31 exons, DNA and amino acid sequence determination and analysis, genetic structure and regulation, the serum response factor myocardin plays a central role in regulating mylk1 gene expression, a highly conserved CArG element within 130-kDa MLCK intron 1 is important for promoter activity binding activation factors like myocardin, homebox proteins, GATA family members, and the thyrotroph embryonic factor, regulation model, overview
-
sequence and expression analysis and comparison, both the mouse and human obscurinassociated kinase-like transcripts also share a conserved putative translation initiation site, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Lactobacillus rhamnosus alleviates intestinal barrier dysfunction in part by increasing expression of myosin light-chain kinase in vivo
-
MLCK expression is significantly up-regulated after controlled cortical impact with a maximum 12 h post-injury
-
severe burn injury increases intestinal MLCK protein levels 3.6fold after 2h in animals resuscitated with normal saline
-
thoracic irradiation significantly augments protein expression and enzymatic activity of the nonmuscle isoform of myosin light chain kinase
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
therapeutic inhibition via specific chemical inhibitors of endothelial isozyme, i.e. 11-(3-chloro-6-immino-6H-pyridazin-1-yl)-undecanoic acid (6-phenyl-pyridazin-3-yl)-amide, represents an important new target for the treatment of inflammatory lung disease with less side effects than other therapies
medicine
-
long isozyme MLCK-210 is a potential therapeutic target in the treatment of burn edema
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Deng, M.; Williams, C.J.; Schultz, R.M.
Role of MAP kinase and myosin light chain kinase in chromosome-induced development of mouse egg polarity
Dev. Biol.
278
358-366
2005
Mus musculus
Tinsley, J.H.; Yuan, S.Y.; Wilson, E.
Isoform-specific knockout of endothelial myosin light chain kinase: closing the gap on inflammatory lung disease
Trends Pharmacol. Sci.
25
64-66
2004
Homo sapiens, Mus musculus
Herring, B.P.; El-Mounayri, O.; Gallagher, P.J.; Yin, F.; Zhou, J.
Regulation of and telokin expression in smooth muscle tissues
Am. J. Physiol.
291
C817-C827
2006
Mus musculus
Gu, L.Z.; Hu, W.Y.; Antic, N.; Mehta, R.; Turner, J.R.; de Lanerolle, P.
Inhibiting myosin light chain kinase retards the growth of mammary and prostate cancer cells
Eur. J. Cancer
42
948-957
2006
Mus musculus, Rattus norvegicus
Connell, L.E.; Helfman, D.M.
Myosin light chain kinase plays a role in the regulation of epithelial cell survival
J. Cell Sci.
119
2269-2281
2006
Mus musculus
Reynoso, R.; Perrin, R.M.; Breslin, J.W.; Daines, D.A.; Watson, K.D.; Watterson, D.M.; Wu, M.H.; Yuan, S.
A role for long chain myosin light chain kinase (MLCK-210) in microvascular hyperpermeability during severe burns
Shock
28
589-595
2007
Mus musculus
Mizuno, Y.; Isotani, E.; Huang, J.; Ding, H.; Stull, J.T.; Kamm, K.E.
Myosin light chain kinase activation and calcium sensitization in smooth muscle in vivo
Am. J. Physiol. Cell Physiol.
295
C358-C364
2008
Mus musculus
Chan, J.Y.; Takeda, M.; Briggs, L.E.; Graham, M.L.; Lu, J.T.; Horikoshi, N.; Weinberg, E.O.; Aoki, H.; Sato, N.; Chien, K.R.; Kasahara, H.
Identification of cardiac-specific myosin light chain kinase
Circ. Res.
102
571-580
2008
Mus musculus (Q6PDN3)
He, W.Q.; Peng, Y.J.; Zhang, W.C.; Lv, N.; Tang, J.; Chen, C.; Zhang, C.H.; Gao, S.; Chen, H.Q.; Zhi, G.; Feil, R.; Kamm, K.E.; Stull, J.T.; Gao, X.; Zhu, M.S.
Myosin light chain kinase is central to smooth muscle contraction and required for gastrointestinal motility in mice
Gastroenterology
135
610-620
2008
Mus musculus
Horman, S.; Morel, N.; Vertommen, D.; Hussain, N.; Neumann, D.; Beauloye, C.; El Najjar, N.; Forcet, C.; Viollet, B.; Walsh, M.P.; Hue, L.; Rider, M.H.
AMP-activated protein kinase phosphorylates and desensitizes smooth muscle myosin light chain kinase
J. Biol. Chem.
283
18505-18512
2008
Mus musculus, Gallus gallus (P11799), Gallus gallus, Rattus norvegicus (P20689)
Borisov, A.B.; Raeker, M.O.; Russell, M.W.
Developmental expression and differential cellular localization of obscurin and obscurin-associated kinase in cardiac muscle cells
J. Cell. Biochem.
103
1621-1635
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Feighery, L.M.; Cochrane, S.W.; Quinn, T.; Baird, A.W.; OToole, D.; Owens, S.E.; ODonoghue, D.; Mrsny, R.J.; Brayden, D.J.
Myosin light chain kinase inhibition: correction of increased intestinal epithelial permeability in vitro
Pharm. Res.
25
1377-1386
2008
Homo sapiens, Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
Zhang, W.C.; Peng, Y.J.; Zhang, G.S.; He, W.Q.; Qiao, Y.N.; Dong, Y.Y.; Gao, Y.Q.; Chen, C.; Zhang, C.H.; Li, W.; Shen, H.H.; Ning, W.; Kamm, K.E.; Stull, J.T.; Gao, X.; Zhu, M.S.
Myosin light chain kinase is necessary for tonic airway smooth muscle contraction
J. Biol. Chem.
285
5522-5531
2010
Mus musculus
Miyauchi, E.; Morita, H.; Tanabe, S.
Lactobacillus rhamnosus alleviates intestinal barrier dysfunction in part by increasing expression of zonula occludens-1 and myosin light-chain kinase in vivo
J. Dairy Sci.
92
2400-2408
2009
Homo sapiens, Mus musculus
Luh, C.; Kuhlmann, C.R.; Ackermann, B.; Timaru-Kast, R.; Luhmann, H.J.; Behl, C.; Werner, C.; Engelhard, K.; Thal, S.C.
Inhibition of myosin light chain kinase reduces brain edema formation after traumatic brain injury
J. Neurochem.
112
1015-1025
2009
Mus musculus
Raina, H.; Zacharia, J.; Li, M.; Wier, W.G.
Activation by Ca2+/calmodulin of an exogenous myosin light chain kinase in mouse arteries
J. Physiol.
587
2599-2612
2009
Mus musculus
Costantini, T.W.; Loomis, W.H.; Putnam, J.G.; Kroll, L.; Eliceiri, B.P.; Baird, A.; Bansal, V.; Coimbra, R.
Pentoxifylline modulates intestinal tight junction signaling after burn injury: effects on myosin light chain kinase
J. Trauma
66
17-24
2009
Mus musculus
McGinnis, L.A.; Lee, H.J.; Robinson, D.N.; Evans, J.P.
MAPK3/1 (ERK1/2) and myosin light chain kinase in mammalian eggs affect myosin-II function and regulate the metaphase II state in a calcium- and zinc-dependent manner
Biol. Reprod.
92
146
2015
Mus musculus (Q3UIZ8), Mus musculus CF-1 (Q3UIZ8)
Chen, C.; Tao, T.; Wen, C.; He, W.Q.; Qiao, Y.N.; Gao, Y.Q.; Chen, X.; Wang, P.; Chen, C.P.; Zhao, W.; Chen, H.Q.; Ye, A.P.; Peng, Y.J.; Zhu, M.S.
Myosin light chain kinase (MLCK) regulates cell migration in a myosin regulatory light chain phosphorylation-independent mechanism
J. Biol. Chem.
289
28478-28488
2014
Mus musculus (Q6PDN3)
Taniguchi, M.; Okamoto, R.; Ito, M.; Goto, I.; Fujita, S.; Konishi, K.; Mizutani, H.; Dohi, K.; Hartshorne, D.J.; Itoh, T.
New isoform of cardiac myosin light chain kinase and the role of cardiac myosin phosphorylation in alpha1-adrenoceptor mediated inotropic response
PLoS ONE
10
e0141130
2015
Mus musculus (Q3UIZ8), Mus musculus, Mus musculus C57BL/6N/C57BL/6J (Q3UIZ8)
Wang, T.; Mathew, B.; Wu, X.; Shimizu, Y.; Rizzo, A.N.; Dudek, S.M.; Weichselbaum, R.R.; Jacobson, J.R.; Hecker, L.; Garcia, J.G.
Nonmuscle myosin light chain kinase activity modulates radiation-induced lung injury
Pulm. Circ.
6
234-239
2016
Mus musculus
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