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 journalArticle

    18 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

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    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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