PPP1R12A

PPP1R12A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KJY, 2MXR, 5HUZ
Identifiers
Aliases	PPP1R12A, M130, MBS, MYPT1, protein phosphatase 1 regulatory subunit 12A
External IDs	MGI: 1309528 HomoloGene: 1855 GeneCards: PPP1R12A
Gene ontology Molecular function • enzyme inhibitor activity • phosphatase regulator activity • 14-3-3 protein binding • signal transducer activity • protein binding • protein kinase binding Cellular component • cytoplasm • cytosol • centrosome • focal adhesion • nucleoplasm • Z disc • PTW/PP1 phosphatase complex • actin cytoskeleton • contractile fiber • A band • kinetochore Biological process • regulation of nucleocytoplasmic transport • positive regulation of myosin-light-chain-phosphatase activity • negative regulation of catalytic activity • mitotic nuclear division • centrosome organization • cellular response to drug • regulation of cell adhesion • G2/M transition of mitotic cell cycle • regulation of myosin-light-chain-phosphatase activity • regulation of establishment of endothelial barrier • positive regulation of transcription from RNA polymerase II promoter • signal transduction • protein dephosphorylation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4659	17931
Ensembl	ENSG00000058272	ENSMUSG00000019907
UniProt	O14974	Q9DBR7
RefSeq (mRNA)	NM_001143885 NM_001143886 NM_001244990 NM_001244992 NM_002480	NM_027892
RefSeq (protein)	NP_001137357.1 NP_001137358.1 NP_001231919.1 NP_001231921.1 NP_002471.1	NP_082168.1
Location (UCSC)	Chr 12: 79.77 – 79.94 Mb	Chr 10: 108.16 – 108.28 Mb
PubMed search	[1]	[2]
Wikidata

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Protein phosphatase 1 regulatory subunit 12A is an enzyme that in humans is encoded by the PPP1R12A gene.^[3][4]

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 ^[5] 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.^[4]

Interactions

PPP1R12A has been shown to interact with Interleukin 16.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "Entrez Gene: PPP1R12A protein phosphatase 1, regulatory (inhibitor) subunit 12A".
5. Michael P. Walsh; et all. "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).
6. 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

• Somlyo AP, Wu X, Walker LA, Somlyo AV (1999). "Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases.". Rev. Physiol. Biochem. Pharmacol. 134: 201–34. doi:10.1007/3-540-64753-8_5. PMID 10087910.
• Ziter FA, Wiser WC, Robinson A (1977). "Three-generation pedigree of a Möbius syndrome variant with chromosome translocation.". Arch. Neurol. 34 (7): 437–42. doi:10.1001/archneur.1977.00500190071011. PMID 880069.
• Slee JJ, Smart RD, Viljoen DL (1991). "Deletion of chromosome 13 in Moebius syndrome.". J. Med. Genet. 28 (6): 413–4. doi:10.1136/jmg.28.6.413. PMC 1016909. PMID 1870098.
• Kimura K, Ito M, Amano M, et al. (1996). "Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)". Science. 273 (5272): 245–8. doi:10.1126/science.273.5272.245. PMID 8662509.
• Ito M, Feng J, Tsujino S, et al. (1997). "Interaction of smooth muscle myosin phosphatase with phospholipids.". Biochemistry. 36 (24): 7607–14. doi:10.1021/bi9702647. PMID 9200713.
• Nakai K, Suzuki Y, Kihira H, et al. (1997). "Regulation of myosin phosphatase through phosphorylation of the myosin-binding subunit in platelet activation.". Blood. 90 (10): 3936–42. PMID 9354661.
• Somlyo AP (1999). "Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser.". J. Physiol. (Lond.). 516 (3): 630. doi:10.1111/j.1469-7793.1999.0630u.x. PMC 2269296. PMID 10200412.
• Surks HK, Mochizuki N, Kasai Y, et al. (1999). "Regulation of myosin phosphatase by a specific interaction with cGMP- dependent protein kinase Ialpha.". Science. 286 (5444): 1583–7. doi:10.1126/science.286.5444.1583. PMID 10567269.
• Feng J, Ito M, Ichikawa K, et al. (2000). "Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase.". J. Biol. Chem. 274 (52): 37385–90. doi:10.1074/jbc.274.52.37385. PMID 10601309.
• Arimura T, Suematsu N, Zhou YB, et al. (2001). "Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit.". J. Biol. Chem. 276 (9): 6073–82. doi:10.1074/jbc.M008566200. PMID 11067852.
• Sebbagh M, Renvoizé C, Hamelin J, et al. (2001). "Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing.". Nat. Cell Biol. 3 (4): 346–52. doi:10.1038/35070019. PMID 11283607.
• Murányi A, Zhang R, Liu F, et al. (2001). "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity.". FEBS Lett. 493 (2-3): 80–4. doi:10.1016/S0014-5793(01)02283-9. PMID 11287000.
• Machida H, Ito M, Okamoto R, et al. (2001). "Molecular cloning and analysis of the 5'-flanking region of the human MYPT1 gene.". Biochim. Biophys. Acta. 1517 (3): 424–9. doi:10.1016/s0167-4781(00)00285-2. PMID 11342221.
• Kiss E, Murányi A, Csortos C, et al. (2002). "Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton.". Biochem. J. 365 (Pt 1): 79–87. doi:10.1042/BJ20011295. PMC 1222641. PMID 11931630.
• Velasco G, Armstrong C, Morrice N, et al. (2002). "Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin.". FEBS Lett. 527 (1-3): 101–4. doi:10.1016/S0014-5793(02)03175-7. PMID 12220642.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Kitazawa T, Eto M, Woodsome TP, Khalequzzaman M (2003). "Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle.". J. Physiol. (Lond.). 546 (Pt 3): 879–89. doi:10.1113/jphysiol.2002.029306. PMC 2342583. PMID 12563012.
• Seko T, Ito M, Kureishi Y, et al. (2003). "Activation of RhoA and inhibition of myosin phosphatase as important components in hypertension in vascular smooth muscle.". Circ. Res. 92 (4): 411–8. doi:10.1161/01.RES.0000059987.90200.44. PMID 12600888.

External links

• PPP1R12A Info with links in the Cell Migration Gateway