Structure and Function of the Cochaperone Prefoldin.
Sign Up to like & getrecommendations! Published in 2018 at "Advances in experimental medicine and biology"
DOI: 10.1007/978-3-030-00737-9_9
Abstract: Molecular chaperones are key players in proteostasis, the balance between protein synthesis, folding, assembly and degradation. They are helped by a plethora of cofactors termed cochaperones, which direct chaperones towards any of these different, sometime… read more here.
Keywords: function cochaperone; cochaperone; cochaperone prefoldin; prefoldin ... See more keywords
HSP70/DNAJA3 chaperone/cochaperone regulates NF-κB activity in immune responses.
Sign Up to like & getrecommendations! Published in 2019 at "Biochemical and biophysical research communications"
DOI: 10.1016/j.bbrc.2019.04.077
Abstract: Nuclear factor kappa B (NF-κB) controls the transcription of various genes in response to immune stimuli. Our previous study revealed that the Droj2/DNAJA3 cochaperone contributes to the NF-κB pathway in Drosophila and humans. In general,… read more here.
Keywords: chaperone cochaperone; hsp70 dnaja3; dnaja3 chaperone; immune responses ... See more keywords
The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.
Sign Up to like & getrecommendations! Published in 2021 at "Molecular cell"
DOI: 10.1016/j.molcel.2021.07.023
Abstract: The Hsp90 chaperone promotes folding and activation of hundreds of client proteins in the cell through an ATP-dependent conformational cycle guided by distinct cochaperone regulators. The FKBP51 immunophilin binds Hsp90 with its tetratricopeptide repeat (TPR)… read more here.
Keywords: hsp90; client; cochaperone; client maturation ... See more keywords
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
Sign Up to like & getrecommendations! Published in 2017 at "Nature Communications"
DOI: 10.1038/s41467-017-02711-w
Abstract: During the Hsp90-mediated chaperoning of protein kinases, the core components of the machinery, Hsp90 and the cochaperone Cdc37, recycle between different phosphorylation states that regulate progression of the chaperone cycle. We show that Cdc37 phosphorylation… read more here.
Keywords: hsp90 phosphorylation; client; cochaperone; client class ... See more keywords
Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle.
Sign Up to like & getrecommendations! Published in 2023 at "PLoS genetics"
DOI: 10.1371/journal.pgen.1010772
Abstract: Molecular chaperones play a key role in maintaining proteostasis and cellular health. The abundant, essential, cytosolic Hsp90 (Heat shock protein, 90 kDa) facilitates the folding and activation of hundreds of newly synthesized or misfolded client… read more here.
Keywords: cycle; closed conformation; hsp90; hsp90 mutants ... See more keywords