EC Number   |
General Information |
Reference |
|---|
   3.1.3.53 | 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 |
714803 |
| 3.1.3.53 | 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 |
732145 |
| 3.1.3.53 | malfunction |
enzyme domain MYPT mutation, MEL-11, causes cytokinesis failure |
713964 |
| 3.1.3.53 | 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 |
732482 |
| 3.1.3.53 | malfunction |
Morpholino knock-down of ppp1cba and ppp1cbb results in severe defects in morphogenetic cell movements during gastrulation through loss of myosin phosphatase function |
732752 |
| 3.1.3.53 | 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 |
713963 |
| 3.1.3.53 | more |
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 |
715574 |
| 3.1.3.53 | more |
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 |
715547 |
| 3.1.3.53 | more |
regulation of the enzyme involving ERM proteins ezrin, radixin, moesin, and isozymes of myosin PPase targeting subunit 1, MYPT1, overview |
715719 |
| 3.1.3.53 | more |
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 |
713963 |
