p202 self-associates through a sequence conserved among the members of the 200-family proteins

Dimpy Koul, Nihal U. Obeyesekere, Jordan U. Gutterman, Gordon B. Mills, Divaker Choubey

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Murine p202 is an interferon-inducible primarily nuclear phosphoprotein (52 kDa) whose expression in transfected cells inhibits colony formation. p202-binding proteins include the pocket proteins (pRb, p107 and p130), a p53-binding protein (sm53BP1), and transcription factors (e.g. NF-κB (p50 and p65), AP-1 (c-Fos and c-Jun), E2F-1, E2F-4, MyoD, and myogenin). p202 modulates the transcriptional activity of these factors in transfected cells. Here we demonstrate that p202 self-associates directly and a sequence in p202, which is conserved among the members of the 200-family proteins, was sufficient for self-association in vitro. Our observations reported herein raise the possibility that self-association of p202 may provide a mechanism for the regulation of its activity. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)21-24
Number of pages4
JournalFEBS Letters
Volume438
Issue number1-2
DOIs
StatePublished - Oct 30 1998
Externally publishedYes

Keywords

  • 200-family proteins
  • Conserved sequence
  • Protein-protein interaction motif
  • Self-association
  • p202

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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