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Nucleotide Exchange Factors for Hsp70 Molecular Chaperones

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Networking of Chaperones by Co-Chaperones

Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

Abstract

Hsp70 molecular chaperones hydrolyze and re-bind ATP concomitant with the binding and release of aggregation-prone protein substrates. As a result, Hsp70s can enhance protein folding and degradation, the assembly of multi-protein complexes, and the catalytic activity of select enzymes. The ability of Hsp70 to perform these diverse functions is regulated by two other classes of proteins: Hsp40s (also known as J-domain-containing proteins) and Hsp70-specific nucleotide exchange factors (NEFs). Although a NEF for a prokaryotic Hsp70, DnaK has been known and studied for some time, eukaryotic Hsp70s NEFs were discovered more recently. Like their Hsp70 partners, the eukaryotic NEFs also play diverse roles in cellular processes, and recent structural studies have elucidated their mechanism of action.

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Authors and Affiliations

  1. Department of Biological Sciences, 274A Crawford Hall, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA

    Jeffrey L. Brodsky

  2. Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany

    Andreas Bracher

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  1. Jeffrey L. Brodsky
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  2. Andreas Bracher
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Brodsky, J.L., Bracher, A. (2007). Nucleotide Exchange Factors for Hsp70 Molecular Chaperones. In: Networking of Chaperones by Co-Chaperones. Molecular Biology Intelligence Unit. Springer, New York, NY. https://doi.org/10.1007/978-0-387-49310-7_1

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