RBL1

RBL1
Retinoblastoma-like protein 1

Vorhandene Strukturdaten: 1h28
Größe 1068 Aminosäuren
Isoformen 2
Bezeichner
Gen-Namen RBL1; PRB1; CP107; MGC40006; p107
Externe IDs OMIM116957 UniProtP28749   MGI103300
Vorkommen
Homologie-Familie RB1
Übergeordnetes Taxon Eukaryoten
Orthologe
Mensch Maus
Entrez 5933 19650
Ensembl ENSG00000080839 ENSMUSG00000027641
UniProt P28749 Q3U1D4
Refseq (mRNA) NM_002895 NM_011249
Refseq (Protein) NP_002886 NP_035379
Genlocus Chr chr20: 35.06 - 35.16 Mb Chr chr2: 156.84 - 156.9 Mb
PubMed Suche [1] [2]

Das Retinoblastoma-like 1 Protein (p107, RBL1) ist ein Protein in Eukaryoten, das an der Regulation des Zellzyklus beteiligt ist. Es ist direkt in die Bildung des Heterochromatin beim Beginn der Zellteilung involviert, indem es die Chromatinstruktur und die Methylierung der Histone kontrolliert. RBL1 ist vermutlich ein Tumorsuppressor.[1]

p107 wird im S/M-Phasenübergang phosphoryliert und in der G1-Phase des Zellzyklus dephosphoryliert. Das RB1-Protein und das RBL1-Protein können mit dem E1A-Protein der Adenoviren und dem large T-antigen von SV40 Komplexe bilden. Das large T-antigen bindet an RB1 und RBL1 nur, wenn diese dephosphoryliert sind. Beide Proteine können die Transkription von Genen inhibieren, die den Zellzyklus regieren und sogenannte E2F-Bindungstellen in ihren Regulationsgenen besitzen.

RBL1 ist in seiner Sequenz und Funktion dem Retinoblastoma-1-Gen ähnlich. Aufgrund der Ähnlichkeit, das RBL1 mit RB1 besitzt, vermutet man, dass RBL1 auch ein Tumorsuppressor ist. Bislang hat man zwei verschiedene Transkripte des Gens entdeckt, die zwei Isoformen des Genproduktes entsprechen.[2]

Siehe auch

Weiterführende Literatur

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

Einzelnachweise

  1. UniProt-Eintrag
  2. Entrez Gene: RBL1 retinoblastoma-like 1 (p107).

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