Bennington College

Folding and Quality Control of the VHL Tumor Suppressor Proceed through Distinct Chaperone Pathways

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dc.contributor.author McClellan, Amie J.
dc.contributor.author Scott, Melissa D.
dc.contributor.author Frydman, Judith
dc.date.accessioned 2016-10-28T19:35:34Z
dc.date.available 2016-10-28T19:35:34Z
dc.date.issued 2005-06
dc.identifier.citation Cell, Vol. 121, 739–748, June 3, 2005, Copyright ©2005 by Elsevier Inc. DOI 10.1016/j.cell.2005.03.024 en_US
dc.identifier.uri http://hdl.handle.net/11209/10521
dc.description.abstract The mechanisms by which molecular chaperones assist quality control of cytosolic proteins are poorly understood. Analysis of the chaperone requirements for degradation of misfolded variants of a cytosolic protein, the VHL tumor suppressor, reveals that distinct chaperone pathways mediate its folding and quality control. While both folding and degradation of VHL require Hsp70, the chaperon in TRiC is essential for folding but is dispensable for degradation. Conversely, the chaperone Hsp90 neither participates in VHL folding nor is required to maintain misfolded VHL solubility but is essential for its degradation. The cochaperone HOP/Sti1p also participates in VHL quality control and may direct the triage decision by bridging the Hsp70-Hsp90 interaction. Our finding that a distinct chaperone complex is uniquely required for quality control provides evidence for active and specific chaperone participation in triage decisions and suggests that a hierarchy of chaperone interactions can control the alternate fates of a cytosolic protein. en_US
dc.language.iso en en_US
dc.publisher Elsevier en_US
dc.subject Heat shock proteins -- Analysis en_US
dc.subject Tumors -- Analysis en_US
dc.subject Proteins -- Analysis en_US
dc.subject Quality control -- Analysis en_US
dc.title Folding and Quality Control of the VHL Tumor Suppressor Proceed through Distinct Chaperone Pathways en_US
dc.type Article en_US


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