PYK2 senses calcium through a disordered dimerization and calmodulin-binding element.
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ABSTRACT:
SUBMITTER: Momin AA
PROVIDER: S-EPMC9363500 | biostudies-literature | 2022 Aug
REPOSITORIES: biostudies-literature
Publications
PYK2 senses calcium through a disordered dimerization and calmodulin-binding element.
Momin Afaque A AA Mendes Tiago T Barthe Philippe P Faure Camille C Hong SeungBeom S Yu Piao P Kadaré Gress G Jaremko Mariusz M Girault Jean-Antoine JA Jaremko Łukasz Ł Arold Stefan T ST
Communications biology 20220809 1
Multidomain kinases use many ways to integrate and process diverse stimuli. Here, we investigated the mechanism by which the protein tyrosine kinase 2-beta (PYK2) functions as a sensor and effector of cellular calcium influx. We show that the linker between the PYK2 kinase and FAT domains (KFL) encompasses an unusual calmodulin (CaM) binding element. PYK2 KFL is disordered and engages CaM through an ensemble of transient binding events. Calcium increases the association by promoting structural c ...[more]
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