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HspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C

Abstract:

Mechanical force-induced conformational changes in proteins underpin a variety of physiological functions, typified in muscle contractile machinery. Mutations in the actin-binding protein filamin C (FLNC) are linked to musculoskeletal pathologies characterized by altered biomechanical properties and sometimes aggregates. HspB1, an abundant molecular chaperone, is prevalent in striated muscle where it is phosphorylated in response to cues including mechanical stress. We report the interaction ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1126/sciadv.aav8421

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Role:
Author
ORCID:
0000-0002-1258-3173
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Role:
Author
ORCID:
0000-0001-5163-2276
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Role:
Author
ORCID:
0000-0003-3301-6810
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Role:
Author
ORCID:
0000-0001-6640-2561
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Publisher:
American Association for the Advancement of Science Publisher's website
Journal:
Science Advances Journal website
Volume:
5
Issue:
5
Article number:
eaav8421
Publication date:
2019-05-22
Acceptance date:
2019-04-16
DOI:
EISSN:
2375-2548
Pmid:
31131323
Source identifiers:
1003255
Language:
English
Keywords:
Pubs id:
pubs:1003255
UUID:
uuid:cea83cfa-0594-47bb-82f3-ddfe457b0bc3
Local pid:
pubs:1003255
Deposit date:
2019-05-29

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