NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems

被引：18

作者：

Biebl, Maximilian M. ^{[1
]}

Delhommel, Florent ^{[1
,2
]}

Faust, Ofrah ^{[3
]}

Zak, Krzysztof M. ^{[2
]}

Agam, Ganesh ^{[4
]}

Guo, Xiaoyan ^{[5
,6
]}

Muehlhofer, Moritz ^{[1
]}

Dahiya, Vinay ^{[1
]}

Hillebrand, Daniela ^{[1
]}

Popowicz, Grzegorz M. ^{[2
]}

Kampmann, Martin ^{[5
,6
]}

Lamb, Don C. ^{[4
]}

Rosenzweig, Rina ^{[3
]}

Sattler, Michael ^{[1
,2
]}

Buchner, Johannes ^{[1
]}

机构：

[1] Tech Univ Munich, Dept Chem, Lichtenbergstr 4, D-85747 Garching, Germany

[2] Helmholtz Zentrum Munchen, Inst Biol Struct, Neuherberg, Germany

[3] Weizmann Inst Sci, Dept Biol Struct, Rehovot, Israel

[4] Ludwig Maximilians Univ Munchen, Dept Chem, Munich, Germany

[5] Univ Calif San Francisco, Inst Neurodegenerat Dis, San Francisco, CA 94143 USA

[6] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA USA

来源：

MOLECULAR CELL | 2022年 / 82卷 / 03期

基金：

欧洲研究理事会;

关键词：

NMR-SPECTROSCOPY; STRUCTURAL-CHARACTERIZATION; PROTEIN; HSP70; BINDING; P53; ARCHITECTURE; REVEALS; ATPASE; CRISPR;

D O I：

10.1016/j.molcel.2021.12.031

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In the eukaryotic cytosol, the Hsp70 and the Hsp90 chaperone machines work in tandem with the maturation of a diverse array of client proteins. The transfer of nonnative clients between these systems is essential to the chaperoning process, but how it is regulated is still not clear. We discovered that NudC is an essential transfer factor with an unprecedented mode of action: NudC interacts with Hsp40 in Hsp40-Hsp70-client complexes and displaces Hsp70. Then, the interaction of NudC with Hsp90 allows the direct transfer of Hsp40-bound clients to Hsp90 for further processing. Consistent with this mechanism, NudC increases client activation in vitro as well as in cells and is essential for cellular viability. Together, our results show the complexity of the cooperation between the major chaperone machineries in the eukaryotic cytosol.

引用

页码：555 / +

页数：23

共 50 条

[1] Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway
Cintron, Nela S.
Toft, David
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (36) : 26235 - 26244
[2] Substrate transfer from the chaperone Hsp70 to Hsp90
Wegele, H
Wandinger, SK
Schmid, AB
Reinstein, J
Buchner, J
JOURNAL OF MOLECULAR BIOLOGY, 2006, 356 (03) : 802 - 811
[3] Death by chaperone HSP90, HSP70 or both?
Powers, Marissa V.
Clarke, Paul A.
Workman, Paul
CELL CYCLE, 2009, 8 (04) : 518 - 526
[4] Model structure of the Hsp70/Hsp40 chaperone complex
Gruschus, JM
Eisenberg, E
Green, LE
Ferretti, JA
PROTEIN SCIENCE, 2004, 13 : 117 - 117
[5] Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery
Morishima, Yoshihiro
Mehta, Ranjit K.
Yoshimura, Miyako
Lau, Miranda
Southworth, Daniel R.
Lawrence, Theodore S.
Pratt, William B.
Nyati, Mukesh K.
Osawa, Yoichi
MOLECULAR PHARMACOLOGY, 2018, 94 (03) : 984 - 991
[6] Mapping the binding interactions between a specialized Hsp70 chaperone and its Hsp40 co-chaperone: a direct role for the Hsp40 HPD motif
Alderson, T.
Kim, Jin
Markley, John
FASEB JOURNAL, 2014, 28 (01):
[7] Molecular chaperone function of mammalian Hsp70 and Hsp40 - a review
Ohtsuka, K
Hata, M
INTERNATIONAL JOURNAL OF HYPERTHERMIA, 2000, 16 (03) : 231 - 245
[8] Structural and Biochemical Properties of Hsp40/Hsp70 Chaperone System
Faust, Ofrah
Rosenzweig, Rina
HSF1 AND MOLECULAR CHAPERONES IN BIOLOGY AND CANCER, 2020, 1243 : 3 - 20
[9] Structural and functional analysis of the Hsp70/Hsp40 chaperone system
Liu, Qinglian
Liang, Ce
Zhou, Lei
PROTEIN SCIENCE, 2020, 29 (02) : 378 - 390
[10] Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System
Luengo, Tania Moran
Kityk, Roman
Mayer, Matthias P.
Rudiger, Stefan G. D.
MOLECULAR CELL, 2018, 70 (03) : 545 - +

← 1 2 3 4 5 →