- Proteína del retinoblastoma-like 2
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Proteína del retinoblastoma-like 2 HUGO 9894 Símbolo RBL2 Símbolos alt. FLJ26459; P130; Rb2 Datos genéticos Locus Cr. 16 q12.2 Bases de datos Entrez 5934 OMIM 180203 RefSeq NP_005602 UniProt Q08999 La proteína del retinoblastoma-like 2 (p130) es un factor de transcripción codificado en humanos por el gen rbl2.[1] [2] Esta proteína pertenece a la familia de proteínas bolsillo.
Contenido
Interacciones
La proteína del retinoblastoma-like 2 ha demostrado ser capaz de interaccionar con:
- HDAC1[3] [4]
- c-Raf[5]
- RBBP8[6] [7]
- Ciclina E1[8] [9]
- Prohibitina[10]
- Cdk2[8] [11]
- BRF1[12]
- BRCA1[13]
Véase también
- Familia de proteínas pocket
Referencias
- ↑ Mayol X, Grana X, Baldi A, Sang N, Hu Q, Giordano A (Sep 1993). «Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain». Oncogene 8 (9): pp. 2561–6. PMID 8361765.
- ↑ Baldi A, Boccia V, Claudio PP, De Luca A, Giordano A (Jul 1996). «Genomic structure of the human retinoblastoma-related Rb2/p130 gene». Proc Natl Acad Sci U S A 93 (10): pp. 4629–32. PMID 8643454.
- ↑ 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): pp. 10493–8. ISSN 0027-8424. PMID 9724731.
- ↑ Bouzahzah, B; Fu M, Iavarone A, Factor V M, Thorgeirsson S S, Pestell R G (Aug. 2000). «Transforming growth factor-beta1 recruits histone deacetylase 1 to a p130 repressor complex in transgenic mice in vivo». Cancer Res. (UNITED STATES) 60 (16): pp. 4531–7. ISSN 0008-5472. PMID 10969803.
- ↑ Wang, S; Ghosh R N, Chellappan S P (Dec. 1998). «Raf-1 physically interacts with Rb and regulates its function: a link between mitogenic signaling and cell cycle regulation». Mol. Cell. Biol. (UNITED STATES) 18 (12): pp. 7487–98. ISSN 0270-7306. PMID 9819434.
- ↑ Meloni, A R; Smith E J, Nevins J R (Aug. 1999). «A mechanism for Rb/p130-mediated transcription repression involving recruitment of the CtBP corepressor». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (17): pp. 9574–9. ISSN 0027-8424. PMID 10449734.
- ↑ Fusco, C; Reymond A, Zervos A S (Aug. 1998). «Molecular cloning and characterization of a novel retinoblastoma-binding protein». Genomics (UNITED STATES) 51 (3): pp. 351–8. doi:. ISSN 0888-7543. PMID 9721205.
- ↑ a b 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): pp. 1460–9. ISSN 0270-7306. PMID 9891079.
- ↑ Li, Y; Graham C, Lacy S, Duncan A M, Whyte P (Dec. 1993). «The adenovirus E1A-associated 130-kD protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins A and E». Genes Dev. (UNITED STATES) 7 (12A): pp. 2366–77. ISSN 0890-9369. PMID 8253383.
- ↑ 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): pp. 3501–10. doi:. ISSN 0950-9232. PMID 10376528.
- ↑ Lacy, S; Whyte P (May. 1997). «Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes». Oncogene (ENGLAND) 14 (20): pp. 2395–406. doi:. ISSN 0950-9232. PMID 9188854.
- ↑ 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): pp. 4255–61. ISSN 0270-7306. PMID 10330166.
- ↑ 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): pp. 4827–41. doi:. ISSN 0950-9232. PMID 11521194.
Enlaces externos
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