The MDM2 RING finger is required for cell cycle-dependent regulation of its protein expression

Gu, L., Ying, H. Q., Zheng, H. W., Murray, S. A., Xiao, Z. X. J. (June 2003) The MDM2 RING finger is required for cell cycle-dependent regulation of its protein expression. Febs Letters, 544 (1-3). pp. 218-222. ISSN 0014-5793

URL: http://www.ncbi.nlm.nih.gov/pubmed/12782320
DOI: 10.1016/s0014-5793(03)00502-7

Abstract

The MDM2 oncoprotein is overexpressed in many human tumors and cancers. MDM2 functions as an E3 ligase for p53 and for itself. MDM2 also interacts with the retinoblastoma protein (1113) and the transcription factor E2F1 to promote cell cycle S-phase entry. Here, we report that MDM2 protein expression is cell cycle-regulated, which is dependent on its RING finger domain and requires Lys446. We show that MDM2 protein is stabilized at S phase. In addition, overexpression of MDM2 results in stimulation of E2F activity and accumulation of cells in S phase. These data suggest that ubiquitination of MDM2 is cell cycle-regulated and that MDM2 may play a role in cell cycle progression. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

Item Type: Paper
Uncontrolled Keywords: MDM2 cell cycle E3 ligase RING finger E2F protein expression ONCOPROTEIN MDM2 C-MYC UBIQUITIN LIGASE S-PHASE P53 PHOSPHORYLATION GENE SUPPRESSION ACTIVATION STABILITY Biochemistry & Molecular Biology Biophysics Cell Biology
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > MDM2
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell cycle
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression
CSHL Authors:
Communities: CSHL labs > Zheng lab
Depositing User: Matt Covey
Date: June 2003
Date Deposited: 22 Aug 2014 15:55
Last Modified: 22 Aug 2014 15:55
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30712

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