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• W2062238060 abstract "Autophagic and proteasomal proteolysis are two major pathways for degradation of cellular constituents. Current models suggest that autophagy is responsible for the nonselective bulk degradation of long-lived proteins and organelles while the proteasome specifically degrades short-lived proteins including misfolded proteins caused by the absence of Hsp90 function. Here, we show that the IkappaB kinase (IKK), an essential activator of NF-kappaB, is selectively degraded by autophagy when Hsp90 is inhibited by geldanamycin (GA), a specific Hsp90 inhibitor showing highly effective anti-tumor activity. We find that in this case inactivation of ubiquitination or proteasome fails to block IKK degradation. However, inhibition of autophagy by an autophagy inhibitor or knockout of Atg5, a key component of the autophagy pathway, significantly rescues IKK from GA-induced degradation. These findings provide the first evidence that an Hsp90 client may be degraded by a mechanism different from the proteasome pathway and establish a molecular link among Hsp90, NF-kappaB and autophagy." @default.
• W2062238060 created "2016-06-24" @default.
• W2062238060 creator A5067815098 @default.
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• W2062238060 date "2006-11-01" @default.
• W2062238060 modified "2023-10-09" @default.
• W2062238060 title "Hsp90 inhibition results in autophagy-mediated proteasome-independent degradation of IκB kinase (IKK)" @default.
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• W2062238060 doi "https://doi.org/10.1038/sj.cr.7310109" @default.
• W2062238060 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17088896" @default.
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