Inhibitors | Comment | Organism | Structure |
---|---|---|---|
microcystin | - |
Rattus norvegicus | |
additional information | two major ROK phosphorylation sites, Thr697 and Thr855, on MYPT1 elicit MLCP inhibition. Phosphorylation of both sites inhibits MLCP activity. MYPT1-T855 phosphorylation may also interfere with the binding of MYPT1 to myosin | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
[myosin light-chain] phosphate + H2O | Rattus norvegicus | substrate is regulatory light chain (LC20) of myosin II, MLCP-mediated dephosphorylation of LC20 at Ser19 | [myosin light-chain] + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylation of MYPT1 is a major mechanism of MLCP regulation. Two major ROK phosphorylation sites, Thr697 and Thr855, on MYPT1 elicit MLCP inhibition. Phosphorylation of both sites inhibits MLCP activity. MYPT1-T855 phosphorylation may also interfere with the binding of MYPT1 to myosin | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
smooth muscle | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[myosin light-chain] phosphate + H2O | - |
Rattus norvegicus | [myosin light-chain] + phosphate | - |
? | |
[myosin light-chain] phosphate + H2O | substrate is regulatory light chain (LC20) of myosin II, MLCP-mediated dephosphorylation of LC20 at Ser19 | Rattus norvegicus | [myosin light-chain] + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | smooth muscle MLCP is a trimeric holoenzyme complex composed of 38 kDa PP1c-delat phosphatase, 110-130 kDa regulatory, myosin-targeting subunit, MYPT1, and a small, 20 kDa M20 subunit, presence of an acid residue cluster and LZ the presence of leucine zipper motifs in the LZ+ MYPT1 splice variant | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
MLCP | - |
Rattus norvegicus |
myosin light chain phosphatase | - |
Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
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 | Rattus norvegicus |
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 | Rattus norvegicus |
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 | Rattus norvegicus |