Amino-terminal domains of c-myc and N-myc proteins mediate binding to the retinoblastoma gene product
- PMID: 1865909
- DOI: 10.1038/352541a0
Amino-terminal domains of c-myc and N-myc proteins mediate binding to the retinoblastoma gene product
Abstract
The proteins encoded by the myc gene family are involved in the control of cell proliferation and differentiation, and aberrant expression of myc proteins has been implicated in the genesis of a variety of neoplasms. In the carboxyl terminus, myc proteins have two domains that encode a basic domain/helix-loop-helix and a leucine zipper motif, respectively. These motifs are involved both in DNA binding and in protein dimerization. In addition, myc protein family members share several regions of highly conserved amino acids in their amino termini that are essential for transformation. We report here that an N-terminal domain present in both the c-myc and N-myc proteins mediates binding to the retinoblastoma gene product, pRb. We show that the human papilloma virus E7 protein competes with c-myc for binding to pRb, indicating that these proteins share overlapping binding sites on pRb. Furthermore, a mutant Rb protein from a human tumour cell line that carried a 35-amino-acid deletion in its C terminus failed to bind to c-myc. Our results suggest that c-myc and pRb cooperate through direct binding to control cell proliferation.
Similar articles
-
Myc protein structure: localization of DNA-binding and protein dimerization domains.Oncogene. 1991 Jan;6(1):93-102. Oncogene. 1991. PMID: 1992448
-
Activation of gene transcription by the amino terminus of the N-Myc protein does not require association with the protein encoded by the retinoblastoma suppressor gene RB1.Oncogene. 1993 Oct;8(10):2833-8. Oncogene. 1993. PMID: 8378092
-
Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins.Nature. 2000 Oct 5;407(6804):592-8. doi: 10.1038/35036504. Nature. 2000. PMID: 11034201
-
The basic region/helix-loop-helix/leucine zipper domain of Myc proto-oncoproteins: function and regulation.Oncogene. 1999 May 13;18(19):2955-66. doi: 10.1038/sj.onc.1202750. Oncogene. 1999. PMID: 10378692 Review.
-
A new bind for Myc.Trends Genet. 1992 Mar;8(3):91-6. doi: 10.1016/0168-9525(92)90196-b. Trends Genet. 1992. PMID: 1579994 Review.
Cited by
-
Activation domains of L-Myc and c-Myc determine their transforming potencies in rat embryo cells.Mol Cell Biol. 1992 Jul;12(7):3130-7. doi: 10.1128/mcb.12.7.3130-3137.1992. Mol Cell Biol. 1992. PMID: 1620120 Free PMC article.
-
Nuclear protein phosphorylation and growth control.Biochem J. 1992 Oct 1;287 ( Pt 1)(Pt 1):1-15. doi: 10.1042/bj2870001. Biochem J. 1992. PMID: 1417761 Free PMC article. Review. No abstract available.
-
Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations.Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6958-62. doi: 10.1073/pnas.89.15.6958. Proc Natl Acad Sci U S A. 1992. PMID: 1495986 Free PMC article.
-
Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation.EMBO J. 1994 Sep 1;13(17):4080-6. doi: 10.1002/j.1460-2075.1994.tb06725.x. EMBO J. 1994. PMID: 8076603 Free PMC article.
-
Differential expression of myc, max and RB1 genes in human gliomas and glioma cell lines.Br J Cancer. 1994 Jan;69(1):16-25. doi: 10.1038/bjc.1994.3. Br J Cancer. 1994. PMID: 8286200 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
