title: The remarkable multivalency of the Hsp70 chaperones.
abstract: Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases.
authors.affiliation: Department of Biological Chemistry, The University of Michigan Medical School, 1500 Medical Center Drive, Ann Arbor, MI, 48109, USA. zuiderwe@umich.edu.
authors.forename: Erik R P
authors.initials: ER
authors.lastname: Zuiderweg
authors.affiliation: Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, 06269, USA.
authors.forename: Lawrence E
authors.initials: LE
authors.lastname: Hightower
authors.affiliation: Institute for Neurodegenerative Disease, University of California at San Francisco, 675 Nelson Rising Lane, San Francisco, CA, 94158, USA.
authors.forename: Jason E
authors.initials: JE
authors.lastname: Gestwicki
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D008055:Lipids / Q000737:chemistry; D008958:Models, Molecular; D004364:Pharmaceutical Preparations / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs
chemical_list: D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D008055:Lipids; D004364:Pharmaceutical Preparations; D000255:Adenosine Triphosphate
keywords: Crystallography; Hsc70; NMR spectroscopy; Protein-drug interactions; Protein-protein interactions; Structural biology