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Article

Mitotic phosphorylation regulates Hsp72 spindle localization by uncoupling ATP binding from substrate release.

Science signaling - 14 Aug 2018

Mukherjee Manjeet, Sabir Sarah, O'Regan Laura, Sampson Josephina, Richards Mark W, Huguenin-Dezot Nicolas, Ault James R, Chin Jason W, Zhuravleva Anastasia, Fry Andrew M, Bayliss Richard

Abstract excerpt

Hsp72 is a member of the 70-kDa heat shock family of molecular chaperones (Hsp70s) that comprise a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD) connected by a linker that couples the exchange of adenosine diphosphate (ADP) for adenosine triphosphate (ATP) with the release of the protein substrate. Mitotic phosphorylation of Hsp72 by the kinase NEK6 at Thr66 located in the NBD promotes the...

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Share to Adenosine Diphosphate
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to NIMA-Related Kinases

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Source

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Identifiers

PMID: 30108182
DOI: 10.1126/scisignal.aao2464
PMCID: PMC6166782

Genes

NEK6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

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