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Hsp70-Hsp110 chaperones deliver ubiquitin-dependent and -independent substrates to the 26S proteasome for proteolysis in yeast
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.ORCID iD: 0000-0001-8948-0685
Number of Authors: 2
2018 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 131, no 6, article id jcs210948Article in journal (Refereed) Published
Abstract [en]

During protein quality control, proteotoxic misfolded proteins are recognized by molecular chaperones, ubiquitylated by dedicated quality control ligases and delivered to the 26S proteasome for degradation. Proteins belonging to the Hsp70 chaperone and Hsp110 (the Hsp70 nucleotide exchange factor) families function in the degradation of misfolded proteins by the ubiquitin-proteasome system via poorly understood mechanisms. Here, we report that the Saccharomyces cerevisiae Hsp110 proteins (Sse1 and Sse2) function in the degradation of Hsp70-associated ubiquitin conjugates at the post-ubiquitylation step and are also required for ubiquitin-independent proteasomal degradation. Hsp110 associates with the 19S regulatory particle of the 26S proteasome and interacts with Hsp70 to f acilitate the delivery of Hsp70 substrates for proteasomal degradation. By using a highly defined ubiquitin-independent proteasome substrate, we show that the mere introduction of a single Hsp70-binding site renders its degradation dependent on Hsp110. The findings define a dedicated and chaperone-dependent pathway for the efficient shuttling of cellular proteins to the proteasome with profound implications for understanding protein quality control and cellular stress management.

Place, publisher, year, edition, pages
2018. Vol. 131, no 6, article id jcs210948
Keyword [en]
Protein degradation, Proteasome, Ubiquitin, Chaperone, Hsp70, Quality control
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-154790DOI: 10.1242/jcs.210948ISI: 000427879400004PubMedID: 29507114OAI: oai:DiVA.org:su-154790DiVA, id: diva2:1198249
Available from: 2018-04-17 Created: 2018-04-17 Last updated: 2018-04-17Bibliographically approved

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Kandasamy, GanapathiAndréasson, Claes
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