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CDC42BPA
Introduction
Serine/threonine-protein kinase MRCK alpha is an enzyme that in humans is encoded by the CDC42BPA gene.[1]
The protein encoded by this gene is a member of the Serine/Threonine protein kinase family. This kinase contains multiple functional domains. Its kinase domain is highly similar to that of the myotonic dystrophy protein kinase (DMPK). This kinase also contains a Rac interactive binding (CRIB) domain, and has been shown to bind CDC42. It may function as a CDC42 downstream effector mediating CDC42 induced peripheral actin formation, and promoting cytoskeletal reorganization. Multiple alternatively spliced transcript variants have been described, and the full-length nature of two of them has been reported.[1]
References
References
External links
External links
- Human CDC42BPA genome location and CDC42BPA gene details page in the UCSC Genome Browser.
Further reading
Further reading
- Zhao Y, Loyer P, Li H, et al. (1997). “Cloning and chromosomal location of a novel member of the myotonic dystrophy family of protein kinases”. J. Biol. Chem. 272 (15): 10013–20. doi:10.1074/jbc.272.15.10013. PMID 9092543.
- Leung T, Chen XQ, Tan I, et al. (1998). “Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization”. Mol. Cell. Biol. 18 (1): 130–40. doi:10.1128/mcb.18.1.130. PMC 121465. PMID 9418861.
- Seki N, Ohira M, Nagase T, et al. (1998). “Characterization of cDNA clones in size-fractionated cDNA libraries from human brain”. DNA Res. 4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID 9455484.
- Moncrieff CL, Bailey ME, Morrison N, Johnson KJ (1999). “Cloning and chromosomal localization of human Cdc42-binding protein kinase beta”. Genomics. 57 (2): 297–300. doi:10.1006/geno.1999.5769. PMID 10198171.
- Edwards DC, Sanders LC, Bokoch GM, Gill GN (1999). “Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics”. Nat. Cell Biol. 1 (5): 253–9. doi:10.1038/12963. PMID 10559936.
- Ohashi K, Nagata K, Maekawa M, et al. (2000). “Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop”. J. Biol. Chem. 275 (5): 3577–82. doi:10.1074/jbc.275.5.3577. PMID 10652353.
- Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). “Shotgun sequencing of the human transcriptome with ORF expressed sequence tags”. Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
- Nakamura N, Oshiro N, Fukata Y, et al. (2000). “Phosphorylation of ERM proteins at filopodia induced by Cdc42”. Genes Cells. 5 (7): 571–81. doi:10.1046/j.1365-2443.2000.00348.x. PMID 10947843.
- Lam LT, Pham YC, Nguyen TM, Morris GE (2000). “Characterization of a monoclonal antibody panel shows that the myotonic dystrophy protein kinase, DMPK, is expressed almost exclusively in muscle and heart”. Hum. Mol. Genet. 9 (14): 2167–73. doi:10.1093/hmg/9.14.2167. PMID 10958655.
- Tan I, Seow KT, Lim L, Leung T (2001). “Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha”. Mol. Cell. Biol. 21 (8): 2767–78. doi:10.1128/MCB.21.8.2767-2778.2001. PMC 86907. PMID 11283256.
- Sumi T, Matsumoto K, Shibuya A, Nakamura T (2001). “Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha”. J. Biol. Chem. 276 (25): 23092–6. doi:10.1074/jbc.C100196200. PMID 11340065.
- Lemercier C, Brocard MP, Puvion-Dutilleul F, et al. (2002). “Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor”. J. Biol. Chem. 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873.
- Dong JM, Leung T, Manser E, Lim L (2003). “Cdc42 antagonizes inductive action of cAMP on cell shape, via effects of the myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) on myosin light chain phosphorylation”. Eur. J. Cell Biol. 81 (4): 231–42. doi:10.1078/0171-9335-00238. PMID 12018391.
- 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.
- Tan I, Cheong A, Lim L, Leung T (2003). “Genomic organization of human myotonic dystrophy kinase-related Cdc42-binding kinase alpha reveals multiple alternative splicing and functional diversity”. Gene. 304: 107–15. doi:10.1016/S0378-1119(02)01185-X. PMID 12568720.
- Wilkinson S, Paterson HF, Marshall CJ (2005). “Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion”. Nat. Cell Biol. 7 (3): 255–61. doi:10.1038/ncb1230. PMID 15723050.
- Cmejla R, Petrak J, Cmejlova J (2006). “A novel iron responsive element in the 3’UTR of human MRCKalpha”. Biochem. Biophys. Res. Commun. 341 (1): 158–66. doi:10.1016/j.bbrc.2005.12.155. PMID 16412980.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). “The DNA sequence and biological annotation of human chromosome 1”. Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
- Lefort K, Mandinova A, Ostano P, et al. (2007). “Notch1 is a p53 target gene involved in human keratinocyte tumor suppression through negative regulation of ROCK1/2 and MRCKalpha kinases”. Genes Dev. 21 (5): 562–77. doi:10.1101/gad.1484707. PMC 1820898. PMID 17344417.