Abstract:
:The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protection from stress-induced misfolding and aggregation of polypeptides in most organisms and are responsible for promoting the stability, folding, and degradation of clients to maintain cellular protein homeostasis. Here, we demonstrate quantitative identification of HSP70 and 71 kDa heat shock cognate (HSC70) clients using a ubiquitin-mediated proximity tagging strategy and show that, despite their high degree of similarity, these enzymes have largely nonoverlapping specificities. Both proteins show a preference for association with newly synthesized polypeptides, but each responds differently to changes in the stoichiometry of proteins in obligate multi-subunit complexes. In addition, expression of an amyotrophic lateral sclerosis (ALS)-associated superoxide dismutase 1 (SOD1) mutant protein induces changes in HSP70 and HSC70 client association and aggregation toward polypeptides with predicted disorder, indicating that there are global effects from a single misfolded protein that extend to many clients within chaperone networks. Together these findings show that the ubiquitin-activated interaction trap (UBAIT) fusion system can efficiently isolate the complex interactome of HSP chaperone family proteins under normal and stress conditions.
journal_name
PLoS Bioljournal_title
PLoS biologyauthors
Ryu SW,Stewart R,Pectol DC,Ender NA,Wimalarathne O,Lee JH,Zanini CP,Harvey A,Huibregtse JM,Mueller P,Paull TTdoi
10.1371/journal.pbio.3000606subject
Has Abstractpub_date
2020-07-20 00:00:00pages
e3000606issue
7eissn
1544-9173issn
1545-7885pii
PBIOLOGY-D-19-03406journal_volume
18pub_type
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