Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping | Zendy

Kamran Rizzolo | Zendy; Jennifer Huen | Zendy; Ashwani Kumar | Zendy; Sadhna Phanse | Zendy; James Vlasblom | Zendy; Yoshito Kakihara | Zendy; Hussein A. Zeineddine | Zendy; Zoran Minić | Zendy; Jamie Snider | Zendy; Wen Wang | Zendy; Carles Pons | Zendy; Thiago Vargas Seraphim | Zendy; Edgar E. Boczek | Zendy; Simon Alberti | Zendy; Michael Costanzo | Zendy; Chad L. Myers | Zendy; Igor Štagljar | Zendy; Charles Boone | Zendy; Mohan Babu | Zendy; Walid A. Houry | Zendy

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Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping

Author(s) -

Kamran Rizzolo,

Jennifer Huen,

Ashwani Kumar,

Sadhna Phanse,

James Vlasblom,

Yoshito Kakihara,

Hussein A. Zeineddine,

Zoran Minić,

Jamie Snider,

Wen Wang,

Carles Pons,

Thiago Vargas Seraphim,

Edgar E. Boczek,

Simon Alberti,

Michael Costanzo,

Chad L. Myers,

Igor Štagljar,

Charles Boone,

Mohan Babu,

Walid A. Houry

Publication year - 2017

Publication title -

cell reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.264

H-Index - 154

eISSN - 2639-1856

pISSN - 2211-1247

DOI - 10.1016/j.celrep.2017.08.074

Subject(s) - chaperone (clinical) , biology , hsp90 , computational biology , saccharomyces cerevisiae , co chaperone , microbiology and biotechnology , heat shock protein , hsp70 , gene , genetics , medicine , pathology

A comprehensive view of molecular chaperone function in the cell was obtained through a systematic global integrative network approach based on physical (protein-protein) and genetic (gene-gene or epistatic) interaction mapping. This allowed us to decipher interactions involving all core chaperones (67) and cochaperones (15) of Saccharomyces cerevisiae. Our analysis revealed the presence of a large chaperone functional supercomplex, which we named the naturally joined (NAJ) chaperone complex, encompassing Hsp40, Hsp70, Hsp90, AAA+, CCT, and small Hsps. We further found that many chaperones interact with proteins that form foci or condensates under stress conditions. Using an in vitro reconstitution approach, we demonstrate condensate formation for the highly conserved AAA+ ATPases Rvb1 and Rvb2, which are part of the R2TP complex that interacts with Hsp90. This expanded view of the chaperone network in the cell clearly demonstrates the distinction between chaperones having broad versus narrow substrate specificities in protein homeostasis.

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