The diverse roles of J-proteins, the obligate Hsp70 co-chaperone.
Hsp70s and J-proteins, which constitute one of the most ubiquitous types of molecular chaperone machineries, function in a wide variety of cellular processes. J-proteins play a central role by stimulating an Hsp70's ATPase activity, thereby stabilizing its interaction with client proteins. However, while all J-proteins serve this core purpose, individual proteins are both structurally and functionally diverse. Some, but not all, J-proteins interact with client polypeptides themselves, facilitating their binding to an Hsp70. Some J-proteins have many client proteins, others only one. Certain J-proteins, while not others, are tethered to particular locations within a cellular compartment, thus "recruiting" Hsp70s to the vicinity of their clients. Here we review recent work on the diverse family of J-proteins, outlining emerging themes concerning their function.
Craig
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University of Wisconsin-Madison, 441E Biochemistry Addition, Department of Biochemistry, 433 Babcock Drive, Madison, 53706 WI, USA. ecraig@wisc.edu
Huang
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Aron
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Andrew
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D000818:Animals; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology*; D017510:Protein Folding; D017434:Protein Structure, Tertiary
D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones