PPP1R12A

Last updated
PPP1R12A
Protein PPP1R12A PDB 1s70.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PPP1R12A , M130, MBS, MYPT1, protein phosphatase 1 regulatory subunit 12A, GUBS
External IDs OMIM: 602021 MGI: 1309528 HomoloGene: 1855 GeneCards: PPP1R12A
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001143885
NM_001143886
NM_001244990
NM_001244992
NM_002480

Contents

NM_027892
NM_001368736
NM_001368737

RefSeq (protein)

NP_001137357
NP_001137358
NP_001231919
NP_001231921
NP_002471

NP_082168
NP_001355665
NP_001355666

Location (UCSC) Chr 12: 79.77 – 79.94 Mb Chr 10: 108 – 108.12 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Protein phosphatase 1 regulatory subunit 12A is an enzyme that in humans is encoded by the PPP1R12A gene. [5] [6]

Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle [7] and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. [6]

Interactions

PPP1R12A has been shown to interact with Interleukin 16. [8]

Related Research Articles

<span class="mw-page-title-main">Smooth muscle</span> Involuntary non-striated muscle

Smooth muscle is an involuntary non-striated muscle, so-called because it has no sarcomeres and therefore no striations. It is divided into two subgroups, single-unit and multiunit smooth muscle. Within single-unit muscle, the whole bundle or sheet of smooth muscle cells contracts as a syncytium.

Biological crosstalk refers to instances in which one or more components of one signal transduction pathway affects another. This can be achieved through a number of ways with the most common form being crosstalk between proteins of signaling cascades. In these signal transduction pathways, there are often shared components that can interact with either pathway. A more complex instance of crosstalk can be observed with transmembrane crosstalk between the extracellular matrix (ECM) and the cytoskeleton.

<span class="mw-page-title-main">Myosin light-chain kinase</span> Class of kinase enzymes

Myosin light-chain kinase also known as MYLK or MLCK is a serine/threonine-specific protein kinase that phosphorylates a specific myosin light chain, namely, the regulatory light chain of myosin II.

<span class="mw-page-title-main">Nicorandil</span> Chemical compound

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<span class="mw-page-title-main">ROCK1</span> Protein

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<span class="mw-page-title-main">PPP1CB</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase PP1-beta catalytic subunit is an enzyme that in humans is encoded by the PPP1CB gene.

<span class="mw-page-title-main">Myosin-light-chain phosphatase</span>

Myosin light-chain phosphatase, also called myosin phosphatase (EC 3.1.3.53; systematic name [myosin-light-chain]-phosphate phosphohydrolase), is an enzyme (specifically a serine/threonine-specific protein phosphatase) that dephosphorylates the regulatory light chain of myosin II:

<span class="mw-page-title-main">Myosin light chain</span> Small polypeptide subunit of myosin

A myosin light chain is a light chain of myosin. Myosin light chains were discovered by Chinese biochemist Cao Tianqin when he was a graduate student at the University of Cambridge in England.

<span class="mw-page-title-main">Protein kinase, AMP-activated, alpha 1</span> Protein-coding gene in the species Homo sapiens

5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.

<span class="mw-page-title-main">AKAP5</span> Protein-coding gene in the species Homo sapiens

A-kinase anchor protein 5 is a protein that in humans is encoded by the AKAP5 gene.

<span class="mw-page-title-main">MYL2</span> Protein-coding gene in the species Homo sapiens

Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (MLC-2) also known as the regulatory light chain of myosin (RLC) is a protein that in humans is encoded by the MYL2 gene. This cardiac ventricular RLC isoform is distinct from that expressed in skeletal muscle (MYLPF), smooth muscle (MYL12B) and cardiac atrial muscle (MYL7).

<span class="mw-page-title-main">PHKG1</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKG1 gene.

<span class="mw-page-title-main">CDC42BPA</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase MRCK alpha is an enzyme that in humans is encoded by the CDC42BPA gene.

<span class="mw-page-title-main">M-RIP</span> Protein-coding gene in the species Homo sapiens

Myosin phosphatase Rho-interacting protein is an enzyme that in humans is encoded by the MPRIP gene.

<span class="mw-page-title-main">PPP1R14A</span> Protein found in humans

Protein phosphatase 1 regulatory subunit 14A also known as CPI-17 is a protein that in humans is encoded by the PPP1R14A gene.

<span class="mw-page-title-main">PPP1R12B</span> Protein-coding gene in the species Homo sapiens

Protein phosphatase 1 regulatory subunit 12B is an enzyme that in humans is encoded by the PPP1R12B gene.

<span class="mw-page-title-main">DUSP16</span> Protein-coding gene in humans

Dual specificity protein phosphatase 16 is an enzyme that in humans is encoded by the DUSP16 gene.

<span class="mw-page-title-main">MYLK</span> Gene of the immunoglobulin superfamily

Myosin light chain kinase, smooth muscle also known as kinase-related protein (KRP) or telokin is an enzyme that in humans is encoded by the MYLK gene.

Fasudil (INN) is a potent Rho-kinase inhibitor and vasodilator. Since it was discovered, it has been used for the treatment of cerebral vasospasm, which is often due to subarachnoid hemorrhage, as well as to improve the cognitive decline seen in stroke patients. It has been found to be effective for the treatment of pulmonary hypertension. It has been demonstrated that fasudil could improve memory in normal mice, identifying the drug as a possible treatment for age-related or neurodegenerative memory loss.

<span class="mw-page-title-main">Rho-associated protein kinase</span>

Rho-associated protein kinase (ROCK) is a kinase belonging to the AGC family of serine-threonine specific protein kinases. It is involved mainly in regulating the shape and movement of cells by acting on the cytoskeleton.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000058272 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000019907 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Takahashi N, Ito M, Tanaka J, Nakano T, Kaibuchi K, Odai H, Takemura K (Nov 1997). "Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21". Genomics. 44 (1): 150–2. doi:10.1006/geno.1997.4859. PMID   9286714.
  6. 1 2 "Entrez Gene: PPP1R12A protein phosphatase 1, regulatory (inhibitor) subunit 12A".
  7. Michael P. Walsh; et al. "Thromboxane A2-induced contraction of rat caudal arterial smooth muscle involves activation of Ca2+ entry and Ca2+sensitization: Rho-associated kinase-mediated phosphorylation of MYPT1 at Thr-855 but not Thr-697" (PDF). Archived from the original (PDF) on 2011-07-13.
  8. Bannert, Norbert; Vollhardt Karin; Asomuddinov Bakhtier; Haag Marion; König Herbert; Norley Stephen; Kurth Reinhard (Oct 2003). "PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits". J. Biol. Chem. United States. 278 (43): 42190–9. doi: 10.1074/jbc.M306669200 . ISSN   0021-9258. PMID   12923170.

Further reading