The Full Wiki

Retinoblastoma-like protein 1: Wikis

Advertisements

Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.

Encyclopedia

From Wikipedia, the free encyclopedia

edit
Retinoblastoma-like 1 (p107)
Identifiers
Symbols RBL1; PRB1; CP107; MGC40006; p107
External IDs OMIM116957 MGI103300 HomoloGene2172 GeneCards: RBL1 Gene
RNA expression pattern
PBB GE RBL1 205296 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5933 19650
Ensembl ENSG00000080839 ENSMUSG00000027641
UniProt P28749 Q3U1D4
RefSeq (mRNA) NM_002895 NM_011249
RefSeq (protein) NP_002886 NP_035379
Location (UCSC) Chr 20:
35.06 - 35.16 Mb
Chr 2:
156.84 - 156.9 Mb
PubMed search [1] [2]

Retinoblastoma-like 1 (p107), also known as RBL1, is a protein which in humans is encoded by the RBL1 gene.[1][2]

Contents

Function

The protein encoded by this gene is similar in sequence and possibly function to the product of the retinoblastoma 1 (RB1) gene. The RB1 gene product is a tumor suppressor protein that appears to be involved in cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with adenovirus E1A protein and SV40 Large T-antigen, with the SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing E2F binding sites in their promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene.[1]

Interactions

Retinoblastoma-like protein 1 has been shown to interact with HDAC1,[3][4] RBBP8,[5][6] E2F1,[7] Cyclin-dependent kinase 2,[8][9] BEGAIN,[6] BRF1,[10] BRCA1,[11] Cyclin A2,[7][12] Prohibitin,[13] MYBL2[14][12] and Mothers against decapentaplegic homolog 3.[15]

See also

References

  1. ^ a b "Entrez Gene: RBL1 retinoblastoma-like 1 (p107)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5933.  
  2. ^ Ewen ME, Xing YG, Lawrence JB, Livingston DM (September 1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell 66 (6): 1155–64. doi:10.1016/0092-8674(91)90038-Z. PMID 1833063.  
  3. ^ Lai, A; Lee J M, Yang W M, DeCaprio J A, Kaelin W G, Seto E, Branton P E (Oct. 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Mol. Cell. Biol. (UNITED STATES) 19 (10): 6632–41. ISSN 0270-7306. PMID 10490602.  
  4. ^ Ferreira, R; Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D (Sep. 1998). "The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (18): 10493–8. ISSN 0027-8424. PMID 9724731.  
  5. ^ Fusco, C; Reymond A, Zervos A S (Aug. 1998). "Molecular cloning and characterization of a novel retinoblastoma-binding protein". Genomics (UNITED STATES) 51 (3): 351–8. doi:10.1006/geno.1998.5368. ISSN 0888-7543. PMID 9721205.  
  6. ^ a b Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.  
  7. ^ a b Dyson, N; Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (Dec. 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". J. Virol. (UNITED STATES) 67 (12): 7641–7. ISSN 0022-538X. PMID 8230483.  
  8. ^ Shanahan, F; Seghezzi W, Parry D, Mahony D, Lees E (Feb. 1999). "Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest". Mol. Cell. Biol. (UNITED STATES) 19 (2): 1460–9. ISSN 0270-7306. PMID 9891079.  
  9. ^ Leng, Xiaohong; Noble Martin, Adams Peter D, Qin Jun, Harper J Wade (Apr. 2002). "Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4". Mol. Cell. Biol. (United States) 22 (7): 2242–54. ISSN 0270-7306. PMID 11884610.  
  10. ^ Sutcliffe, J E; Cairns C A, McLees A, Allison S J, Tosh K, White R J (Jun. 1999). "RNA polymerase III transcription factor IIIB is a target for repression by pocket proteins p107 and p130". Mol. Cell. Biol. (UNITED STATES) 19 (6): 4255–61. ISSN 0270-7306. PMID 10330166.  
  11. ^ Fan, S; Yuan R, Ma Y X, Xiong J, Meng Q, Erdos M, Zhao J N, Goldberg I D, Pestell R G, Rosen E M (Aug. 2001). "Disruption of BRCA1 LXCXE motif alters BRCA1 functional activity and regulation of RB family but not RB protein binding". Oncogene (England) 20 (35): 4827–41. doi:10.1038/sj.onc.1204666. ISSN 0950-9232. PMID 11521194.  
  12. ^ a b Joaquin, Manel; Bessa Maria, Saville Mark K, Watson Roger J (Nov. 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene (England) 21 (52): 7923–32. doi:10.1038/sj.onc.1206001. ISSN 0950-9232. PMID 12439743.  
  13. ^ Wang, S; Nath N, Adlam M, Chellappan S (Jun. 1999). "Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function". Oncogene (ENGLAND) 18 (23): 3501–10. doi:10.1038/sj.onc.1202684. ISSN 0950-9232. PMID 10376528.  
  14. ^ Joaquin, Manel; Watson Roger J (Nov. 2003). "The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain". J. Biol. Chem. (United States) 278 (45): 44255–64. doi:10.1074/jbc.M308953200. ISSN 0021-9258. PMID 12947099.  
  15. ^ Chen, Chang-Rung; Kang Yibin, Siegel Peter M, Massagué Joan (Jul. 2002). "E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression". Cell (United States) 110 (1): 19–32. ISSN 0092-8674. PMID 12150994.  

Further reading

  • Faha B, Ewen ME, Tsai LH, et al. (1992). "Interaction between human cyclin A and adenovirus E1A-associated p107 protein.". Science 255 (5040): 87–90. doi:10.1126/science.1532458. PMID 1532458.  
  • Ewen ME, Xing YG, Lawrence JB, Livingston DM (1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein.". Cell 66 (6): 1155–64. doi:10.1016/0092-8674(91)90038-Z. PMID 1833063.  
  • Datta PK, Raychaudhuri P, Bagchi S (1995). "Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription.". Mol. Cell. Biol. 15 (10): 5444–52. PMID 7565695.  
  • Zhu L, Zhu L, Xie E, Chang LS (1995). "Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins.". Mol. Cell. Biol. 15 (7): 3552–62. PMID 7791762.  
  • Sardet C, Vidal M, Cobrinik D, et al. (1995). "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle.". Proc. Natl. Acad. Sci. U.S.A. 92 (6): 2403–7. doi:10.1073/pnas.92.6.2403. PMID 7892279.  
  • Kim YW, Otterson GA, Kratzke RA, et al. (1994). "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein.". Mol. Cell. Biol. 14 (11): 7256–64. PMID 7935440.  
  • Ginsberg D, Vairo G, Chittenden T, et al. (1994). "E2F-4, a new member of the E2F transcription factor family, interacts with p107.". Genes Dev. 8 (22): 2665–79. doi:10.1101/gad.8.22.2665. PMID 7958924.  
  • Beijersbergen RL, Kerkhoven RM, Zhu L, et al. (1994). "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo.". Genes Dev. 8 (22): 2680–90. doi:10.1101/gad.8.22.2680. PMID 7958925.  
  • Beijersbergen RL, Hijmans EM, Zhu L, Bernards R (1994). "Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation.". Embo J. 13 (17): 4080–6. PMID 8076603.  
  • Dyson N, Dembski M, Fattaey A, et al. (1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1.". J. Virol. 67 (12): 7641–7. PMID 8230483.  
  • Zhu L, van den Heuvel S, Helin K, et al. (1993). "Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein.". Genes Dev. 7 (7A): 1111–25. doi:10.1101/gad.7.7a.1111. PMID 8319904.  
  • Ikeda MA, Jakoi L, Nevins JR (1996). "A unique role for the Rb protein in controlling E2F accumulation during cell growth and differentiation.". Proc. Natl. Acad. Sci. U.S.A. 93 (8): 3215–20. doi:10.1073/pnas.93.8.3215. PMID 8622916.  
  • Xiao ZX, Ginsberg D, Ewen M, Livingston DM (1996). "Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases.". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 4633–7. doi:10.1073/pnas.93.10.4633. PMID 8643455.  
  • Vidal M, Brachmann RK, Fattaey A, et al. (1996). "Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions.". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10315–20. doi:10.1073/pnas.93.19.10315. PMID 8816797.  
  • Shao Z, Siegert JL, Ruppert S, Robbins PD (1997). "Rb interacts with TAF(II)250/TFIID through multiple domains.". Oncogene 15 (4): 385–92. doi:10.1038/sj.onc.1201204. PMID 9242374.  
  • Verona R, Moberg K, Estes S, et al. (1997). "E2F activity is regulated by cell cycle-dependent changes in subcellular localization.". Mol. Cell. Biol. 17 (12): 7268–82. PMID 9372959.  
  • Trimarchi JM, Fairchild B, Verona R, et al. (1998). "E2F-6, a member of the E2F family that can behave as a transcriptional repressor.". Proc. Natl. Acad. Sci. U.S.A. 95 (6): 2850–5. doi:10.1073/pnas.95.6.2850. PMID 9501179.  
  • Sterner JM, Dew-Knight S, Musahl C, et al. (1998). "Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7.". Mol. Cell. Biol. 18 (5): 2748–57. PMID 9566894.  
  • Woitach JT, Zhang M, Niu CH, Thorgeirsson SS (1998). "A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability.". Nat. Genet. 19 (4): 371–4. doi:10.1038/1258. PMID 9697699.  
  • Veal E, Eisenstein M, Tseng ZH, Gill G (1998). "A cellular repressor of E1A-stimulated genes that inhibits activation by E2F.". Mol. Cell. Biol. 18 (9): 5032–41. PMID 9710587.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Advertisements

Advertisements






Got something to say? Make a comment.
Your name
Your email address
Message