PPP1R12A

Revision as of 13:33, 6 September 2012 by WikiBot (talk | contribs) (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search


Protein phosphatase 1, regulatory (inhibitor) subunit 12A
File:PBB Protein PPP1R12A image.jpg
PDB rendering based on 1s70.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PPP1R12A ; MBS; MGC133042; MYPT1
External IDs Template:OMIM5 Template:MGI HomoloGene1855
RNA expression pattern
File:PBB GE PPP1R12A 201603 at tn.png
File:PBB GE PPP1R12A 201602 s at tn.png
File:PBB GE PPP1R12A 201604 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Protein phosphatase 1, regulatory (inhibitor) subunit 12A, also known as PPP1R12A, is a human gene.[1]

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 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.[1]

References

  1. 1.0 1.1 "Entrez Gene: PPP1R12A protein phosphatase 1, regulatory (inhibitor) subunit 12A".

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. 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. PMID 880069.
  • Slee JJ, Smart RD, Viljoen DL (1991). "Deletion of chromosome 13 in Moebius syndrome". J. Med. Genet. 28 (6): 413–4. 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. 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.
  • Takahashi N, Ito M, Tanaka J; et al. (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.
  • 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 ( Pt 3): 630. 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. 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. 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. 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. 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. 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. 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. 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. 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.

Template:WikiDoc Sources