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Literature summary for 3.1.3.53 extracted from

  • Cole, W.C.; Welsh, D.G.
    Role of myosin light chain kinase and myosin light chain phosphatase in the resistance arterial myogenic response to intravascular pressure (2011), Arch. Biochem. Biophys., 510, 160-173.
    View publication on PubMed

Inhibitors

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

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

Source Tissue Comment Organism Textmining
smooth muscle
-
Rattus norvegicus
-

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
MLCP
-
Rattus norvegicus
myosin light chain phosphatase
-
Rattus norvegicus

General Information

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