RCHY1
From Wikipedia, the free encyclopedia
RING finger and CHY zinc finger domain-containing protein 1 is a protein that in humans is encoded by the RCHY1 gene.[1]
The protein encoded by this gene has ubiquitin-protein ligase activity. This protein binds with p53 and promotes the ubiquitin-mediated proteosomal degradation of p53. This gene is oncogenic because loss of p53 function contributes directly to malignant tumor development. Transcription of this gene is regulated by p53. Alternative splicing results in multiple transcript variants encoding different isoforms.[1]
Interactions
RCHY1 has been shown to interact with P53[2][3] and Androgen receptor.[4]
References
- ↑ 1.0 1.1 "Entrez Gene: RCHY1 ring finger and CHY zinc finger domain containing 1".
- ↑ Leng, Roger P; Lin Yunping, Ma Weili, Wu Hong, Lemmers Benedicte, Chung Stephen, Parant John M, Lozano Guillermina, Hakem Razqallah, Benchimol Samuel (Mar 2003). "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation". Cell (United States) 112 (6): 779–91. doi:10.1016/S0092-8674(03)00193-4. ISSN 0092-8674. PMID 12654245.
- ↑ Sheng, Yi; Laister Rob C, Lemak Alexander, Wu Bin, Tai Elizabeth, Duan Shili, Lukin Jonathan, Sunnerhagen Maria, Srisailam Sampath, Karra Murthy, Benchimol Sam, Arrowsmith Cheryl H (Dec 2008). "Molecular basis of Pirh2-mediated p53 ubiquitylation". Nat. Struct. Mol. Biol. (United States) 15 (12): 1334–42. doi:10.1038/nsmb.1521. PMID 19043414.
- ↑ Beitel, L K; Elhaji Y A, Lumbroso R, Wing S S, Panet-Raymond V, Gottlieb B, Pinsky L, Trifiro M A (Aug 2002). "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity". J. Mol. Endocrinol. (England) 29 (1): 41–60. doi:10.1677/jme.0.0290041. ISSN 0952-5041. PMID 12200228.
Further reading
- 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.
- Beitel LK, Elhaji YA, Lumbroso R, et al. (2002). "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity". J. Mol. Endocrinol. 29 (1): 41–60. doi:10.1677/jme.0.0290041. PMID 12200228.
- 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.
- Leng RP, Lin Y, Ma W, et al. (2003). "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation". Cell 112 (6): 779–91. doi:10.1016/S0092-8674(03)00193-4. PMID 12654245.
- Logan IR, Sapountzi V, Gaughan L, et al. (2004). "Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome". J. Biol. Chem. 279 (12): 11696–704. doi:10.1074/jbc.M312712200. PMID 14701804.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Corcoran CA, Huang Y, Sheikh MS (2005). "The p53 paddy wagon: COP1, Pirh2 and MDM2 are found resisting apoptosis and growth arrest". Cancer Biol. Ther. 3 (8): 721–5. PMID 15280670.
- Duan W, Gao L, Druhan LJ, et al. (2004). "Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer". J. Natl. Cancer Inst. 96 (22): 1718–21. doi:10.1093/jnci/djh292. PMID 15547185.
- Zhang L, Li J, Wang C, et al. (2005). "A new human gene hNTKL-BP1 interacts with hPirh2". Biochem. Biophys. Res. Commun. 330 (1): 293–7. doi:10.1016/j.bbrc.2005.02.156. PMID 15781263.
- Logan IR, Gaughan L, McCracken SR, et al. (2006). "Human PIRH2 Enhances Androgen Receptor Signaling through Inhibition of Histone Deacetylase 1 and Is Overexpressed in Prostate Cancer". Mol. Cell. Biol. 26 (17): 6502–10. doi:10.1128/MCB.00147-06. PMC 1592843. PMID 16914734.
- Duan W, Gao L, Wu X, et al. (2006). "Differential response between the p53 ubiquitin-protein ligases Pirh2 and MdM2 following DNA damage in human cancer cells". Exp. Cell Res. 312 (17): 3370–8. doi:10.1016/j.yexcr.2006.07.005. PMID 16934800.
- Duan S, Yao Z, Hou D, et al. (2007). "Phosphorylation of Pirh2 by Calmodulin-dependent kinase II impairs its ability to ubiquitinate p53". EMBO J. 26 (13): 3062–74. doi:10.1038/sj.emboj.7601749. PMC 1914097. PMID 17568776.
- Hattori T, Isobe T, Abe K, et al. (2007). "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1". Cancer Res. 67 (22): 10789–95. doi:10.1158/0008-5472.CAN-07-2033. PMID 18006823.
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