PYK2 senses calcium through a disordered dimerization and calmodulin-binding element

Affiliations

Afaque A. Momin: Computational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)
Tiago Mendes: Inserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à Moulin
Philippe Barthe: Centre de Biologie Structurale (CBS), University Montpellier
Camille Faure: Inserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à Moulin
SeungBeom Hong: Computational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)
Piao Yu: Computational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)
Gress Kadaré: Inserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à Moulin
Mariusz Jaremko: Bioscience Program, Division of Biological and Environmental Science and Engineering (BESE), King Abdullah University of Science and Technology (KAUST)
Jean-Antoine Girault: Inserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à Moulin
Łukasz Jaremko: Bioscience Program, Division of Biological and Environmental Science and Engineering (BESE), King Abdullah University of Science and Technology (KAUST)
Stefan T. Arold: Computational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)

Abstract

Protein tyrosine kinase 2-beta is shown to function as a sensor and effector of cellular calcium influx through self-association.