Hsp40 Couples with the CSPα Chaperone Complex upon Induction of the Heat Shock Response

Sarah J Gibbs; Brandy Barren; Katy E Beck; Juliane Proft; Xiaoxi Zhao; Tatiana Noskova; Andrew P Braun; Nikolai O Artemyev; Janice E. A Braun

doi:10.1371/journal.pone.0004595

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Hsp40 Couples with the CSPα Chaperone Complex upon Induction of the Heat Shock Response

Journal article

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Hsp40 Couples with the CSPα Chaperone Complex upon Induction of the Heat Shock Response

Sarah J Gibbs, Brandy Barren, Katy E Beck, Juliane Proft, Xiaoxi Zhao, Tatiana Noskova, Andrew P Braun, Nikolai O Artemyev and Janice E. A Braun

PloS one, Vol.4(2), e4595

02/26/2009

DOI: 10.1371/journal.pone.0004595

PMCID: PMC2643527

PMID: 19242542

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Abstract

In response to a conditioning stress, the expression of a set of molecular chaperones called heat shock proteins is increased. In neurons, stress-induced and constitutively expressed molecular chaperones protect against damage induced by ischemia and neurodegenerative diseases, however the molecular basis of this protection is not known. Here we have investigated the crosstalk between stress-induced chaperones and cysteine string protein (CSPα). CSPα is a constitutively expressed synaptic vesicle protein bearing a J domain and a cysteine rich “string” region that has been implicated in the long term functional integrity of synaptic transmission and the defense against neurodegeneration. We have shown previously that the CSPα chaperone complex increases isoproterenol-mediated signaling by stimulating GDP/GTP exchange of Gαs. In this report we demonstrate that in response to heat shock or treatment with the Hsp90 inhibitor geldanamycin, the J protein Hsp40 becomes a major component of the CSPα complex. Association of Hsp40 with CSPα decreases CSPα-CSPα dimerization and enhances the CSPα-induced increase in steady state GTP hydrolysis of Gαs. This newly identified CSPα-Hsp40 association reveals a previously undescribed coupling of J proteins. In view of the crucial importance of stress-induced chaperones in the protection against cell death, our data attribute a role for Hsp40 crosstalk with CSPα in neuroprotection.

Neurological Disorders

Neuroscience

Cell Biology

Neuronal Signaling Mechanisms

Cellular Death and Stress Responses

Cell Signaling

Neurobiology of Disease and Regeneration

Details

Title: Subtitle: Hsp40 Couples with the CSPα Chaperone Complex upon Induction of the Heat Shock Response
Creators: Sarah J Gibbs
Brandy Barren
Katy E Beck
Juliane Proft
Xiaoxi Zhao
Tatiana Noskova
Andrew P Braun
Nikolai O Artemyev
Janice E. A Braun
Resource Type: Journal article
Publication Details: PloS one, Vol.4(2), e4595
DOI: 10.1371/journal.pone.0004595
PMID: 19242542
PMCID: PMC2643527
NLM abbreviation: PLoS One
ISSN: 1932-6203
eISSN: 1932-6203
Publisher: Public Library of Science; San Francisco, USA
Alternative title: Hsp40/CSPα Chaperone Complex
Language: English
Date published: 02/26/2009
Academic Unit: Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Ophthalmology and Visual Sciences
Record Identifier: 9984025469702771

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