M-RIP

MPRIP
Identifiers
Aliases	MPRIP , M-RIP, MRIP, RHOIP3, RIP3, p116Rip, myosin phosphatase Rho interacting protein
External IDs	OMIM: 612935 MGI: 1349438 HomoloGene: 9034 GeneCards: MPRIP
Gene location (Human)
Chr.	Chromosome 17 (human)
End	17,217,679 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	59,671,686 bp
RNA expression pattern
	Top expressed in
	popliteal artery; ; sural nerve; ; right coronary artery; ; amniotic fluid; ; olfactory bulb; ; saphenous vein; ; ganglionic eminence; ; ascending aorta; ; left coronary artery; ; inferior olivary nucleus;
	Top expressed in
	spermatid; ; ankle joint; ; entorhinal cortex; ; left lung; ; seminiferous tubule; ; right lung; ; spermatocyte; ; left lung lobe; ; superior frontal gyrus; ; right lung lobe;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	actin binding ; protein binding ; cadherin binding ;
Cellular component	cytoskeleton ; focal adhesion ; actin cytoskeleton ; cytoplasm ; cytosol ;
Biological process	cell-cell adhesion ;
	Sources:Amigo / QuickGO
Orthologs
	23164
	26936
	ENSG00000133030
	ENSMUSG00000005417
	Q6WCQ1
	P97434
	NM_015134 ; NM_201274 ; NM_001364716
	NM_012027 ; NM_201245 ; NM_001368931
	NP_055949 ; NP_958431 ; NP_001351645
	NP_036157 ; NP_957697 ; NP_001355860
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 05, 2024

Myosin phosphatase Rho-interacting protein is an enzyme that in humans is encoded by the MPRIP gene.^[5]^[6]

Interactions

M-RIP has been shown to interact with RHOA.^[7]

Related Research Articles

Transforming protein RhoA, also known as Ras homolog family member A (RhoA), is a small GTPase protein in the Rho family of GTPases that in humans is encoded by the RHOA gene. While the effects of RhoA activity are not all well known, it is primarily associated with cytoskeleton regulation, mostly actin stress fibers formation and actomyosin contractility. It acts upon several effectors. Among them, ROCK1 and DIAPH1 are the best described. RhoA, and the other Rho GTPases, are part of a larger family of related proteins known as the Ras superfamily, a family of proteins involved in the regulation and timing of cell division. RhoA is one of the oldest Rho GTPases, with homologues present in the genomes since 1.5 billion years. As a consequence, RhoA is somehow involved in many cellular processes which emerged throughout evolution. RhoA specifically is regarded as a prominent regulatory factor in other functions such as the regulation of cytoskeletal dynamics, transcription, cell cycle progression and cell transformation.

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References

1 2 3 GRCh38: Ensembl release 89: ENSG00000133030 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005417 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (May 1999). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355–64. doi: 10.1093/dnares/5.6.355 . PMID 10048485.
↑ "Entrez Gene: M-RIP myosin phosphatase-Rho interacting protein".
↑ Gebbink MF, Kranenburg O, Poland M, van Horck FP, Houssa B, Moolenaar WH (Jun 1997). "Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: control of neuronal morphology". J. Cell Biol. 137 (7): 1603–13. doi:10.1083/jcb.137.7.1603. PMC 2137826 . PMID 9199174.

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID 8889548.
Gebbink MF, Kranenburg O, Poland M, van Horck FP, Houssa B, Moolenaar WH (1997). "Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: control of neuronal morphology". J. Cell Biol. 137 (7): 1603–13. doi:10.1083/jcb.137.7.1603. PMC 2137826 . PMID 9199174.
Surks HK, Richards CT, Mendelsohn ME (2004). "Myosin phosphatase-Rho interacting protein. A new member of the myosin phosphatase complex that directly binds RhoA". J. Biol. Chem. 278 (51): 51484–93. doi: 10.1074/jbc.M305622200 . PMID 14506264.
Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. Bibcode:2004CBio...14.1436J. doi: 10.1016/j.cub.2004.07.051 . PMID 15324660. S2CID 2371325.
Mulder J, Ariaens A, van den Boomen D, Moolenaar WH (2005). "p116Rip targets myosin phosphatase to the actin cytoskeleton and is essential for RhoA/ROCK-regulated neuritogenesis". Mol. Biol. Cell. 15 (12): 5516–27. doi:10.1091/mbc.E04-04-0275. PMC 532030 . PMID 15469989.
Koga Y, Ikebe M (2005). "p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA". J. Biol. Chem. 280 (6): 4983–91. doi: 10.1074/jbc.M410909200 . PMID 15545284.
Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi: 10.1074/mcp.M500021-MCP200 . PMID 15778465.
Surks HK, Riddick N, Ohtani K (2006). "M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells". J. Biol. Chem. 280 (52): 42543–51. doi: 10.1074/jbc.M506863200 . PMID 16257966.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID 17081983. S2CID 7827573.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948 . PMID 17353931.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000133030 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005417 - 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.

[pmid10048485-5] Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (May 1999). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355–64. doi: 10.1093/dnares/5.6.355 . PMID 10048485.

[entrez-6] "Entrez Gene: M-RIP myosin phosphatase-Rho interacting protein".

[pmid9199174-7] Gebbink MF, Kranenburg O, Poland M, van Horck FP, Houssa B, Moolenaar WH (Jun 1997). "Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: control of neuronal morphology". J. Cell Biol. 137 (7): 1603–13. doi:10.1083/jcb.137.7.1603. PMC 2137826 . PMID 9199174.

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M-RIP

Contents

Interactions

Related Research Articles

References

Further reading