HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor

Mehdi Kabani, Catherine McLellan, Deborah A. Raynes, Vince Guerriero, Jeffrey L. Brodsky

    Research output: Contribution to journalArticlepeer-review

    89 Scopus citations

    Abstract

    The yeast FES1 and SLS1 genes encode conserved nucleotide exchange factors that act on the cytoplasmic and endoplasmic reticulum luminal Hsp70s, Ssa1p and BiP, respectively. We report here that mammalian HspBP1 is homologous to Fes1p and that HspBP1 promotes nucleotide dissociation from both Ssa1p and mammalian Hsc70. In contrast, Fes1p inefficiently strips nucleotide from mammalian Hsc70, and unlike HspBP1 does not inhibit chaperone-mediated protein refolding in vitro. Together, our data indicate that HspBP1 is a member of this new class of nucleotide exchange factors that exhibit varying degrees of compartment and species specificity.

    Original languageEnglish (US)
    Pages (from-to)339-342
    Number of pages4
    JournalFEBS Letters
    Volume531
    Issue number2
    DOIs
    StatePublished - Nov 6 2002

    Keywords

    • Fes1p
    • Hsc70
    • Hsp70
    • HspBP1
    • Nucleotide exchange
    • Sls1p

    ASJC Scopus subject areas

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

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