Journal
ONCOTARGET
Volume 6, Issue 21, Pages 18276-18281Publisher
IMPACT JOURNALS LLC
DOI: 10.18632/oncotarget.4954
Keywords
Hsp70/90 chaperone cycle; co-chaperones; client proteins; mass spectrometry; cross-linking
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Funding
- ERC [268851]
- Wellcome Trust [WT008150, WT099141]
- MRC [98101]
- Engineering and Physical Sciences Research Council [1379038] Funding Source: researchfish
- European Research Council (ERC) [268851] Funding Source: European Research Council (ERC)
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The Hsp70/Hsp90 chaperone cycles depend on the coordinated interplay of several co-chaperones including Hsp40, Hop and peptidyl-prolyl isomerases such as FKBP52. Because of the many proteins involved in these interactions it is often difficult to delineate all possible combinations of subunits in the complexes formed. We employed mass spectrometry to monitor the assembly and to determine the favoured pathways within these chaperone cycles. Combining the subunit composition with chemical cross-linking and proteomics allowed us to define interaction interfaces, protein dynamics and new intermediates.
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