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The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Gestaut, Daniel | - |
dc.contributor.author | Roh, Soung Hun | - |
dc.contributor.author | Ma, Boxue | - |
dc.contributor.author | Pintilie, Grigore | - |
dc.contributor.author | Joachimiak, Lukasz A. | - |
dc.contributor.author | Leitner, Alexander | - |
dc.contributor.author | Walzthoeni, Thomas | - |
dc.contributor.author | Aebersold, Ruedi | - |
dc.contributor.author | Chiu, Wah | - |
dc.contributor.author | Frydman, Judith | - |
dc.date.accessioned | 2024-05-16T01:51:56Z | - |
dc.date.available | 2024-05-16T01:51:56Z | - |
dc.date.created | 2020-04-27 | - |
dc.date.created | 2020-04-27 | - |
dc.date.issued | 2019-04 | - |
dc.identifier.citation | Cell, Vol.177 No.3, pp.751-765.e15 | - |
dc.identifier.issn | 0092-8674 | - |
dc.identifier.uri | https://hdl.handle.net/10371/202932 | - |
dc.description.abstract | Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microscopy (cryo-EM), crosslinking-masss-pectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD. We find these hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates. The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis. | - |
dc.language | 영어 | - |
dc.publisher | Cell Press | - |
dc.title | The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.cell.2019.03.012 | - |
dc.citation.journaltitle | Cell | - |
dc.identifier.wosid | 000464947700026 | - |
dc.identifier.scopusid | 2-s2.0-85064154435 | - |
dc.citation.endpage | 765.e15 | - |
dc.citation.number | 3 | - |
dc.citation.startpage | 751 | - |
dc.citation.volume | 177 | - |
dc.description.isOpenAccess | N | - |
dc.contributor.affiliatedAuthor | Roh, Soung Hun | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | IN-VIVO | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordPlus | COMPLEXES | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | ACTIN | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | AGGREGATION | - |
dc.subject.keywordPlus | POLYPEPTIDE | - |
dc.subject.keywordPlus | REFINEMENT | - |
dc.subject.keywordAuthor | CCT | - |
dc.subject.keywordAuthor | chaperone | - |
dc.subject.keywordAuthor | chaperonin | - |
dc.subject.keywordAuthor | cryo-EM | - |
dc.subject.keywordAuthor | GIMc | - |
dc.subject.keywordAuthor | prefoldin | - |
dc.subject.keywordAuthor | proteostasis | - |
dc.subject.keywordAuthor | TRiC | - |
dc.subject.keywordAuthor | XL-MS | - |
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