Dynamin and PTP-PEST cooperatively regulate Pyk2 dephosphorylation in osteoclasts.

The International Journal of Biochemistry & Cell Biology
Pierre P ElenisteAngela Bruzzaniti

Abstract

Bone loss is caused by the dysregulated activity of osteoclasts which degrade the extracellular bone matrix. The tyrosine kinase Pyk2 is highly expressed in osteoclasts, and mice lacking Pyk2 exhibit an increase in bone mass, in part due to impairment of osteoclast function. Pyk2 is activated by phosphorylation at Y402 following integrin activation, but the mechanisms leading to Pyk2 dephosphorylation are poorly understood. In the current study, we examined the mechanism of action of the dynamin GTPase on Pyk2 dephosphorylation. Our studies reveal a novel mechanism for the interaction of Pyk2 with dynamin, which involves the binding of Pyk2's FERM domain with dynamin's plextrin homology domain. In addition, we demonstrate that the dephosphorylation of Pyk2 requires dynamin's GTPase activity and is mediated by the tyrosine phosphatase PTP-PEST. The dephosphorylation of Pyk2 by dynamin and PTP-PEST may be critical for terminating outside-in integrin signaling, and for stabilizing cytoskeletal reorganization during osteoclast bone resorption.

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Citations

Apr 24, 2013·Journal of Molecular Medicine : Official Organ of the Gesellschaft Deutscher Naturforscher Und Ärzte·Laura BriñasMarc Bitoun
Aug 14, 2012·Journal of Signal Transduction·Pierre P Eleniste, Angela Bruzzaniti
Apr 4, 2014·Molecular Biology of the Cell·Eynat FinkelshteinAri Elson
Nov 11, 2015·Journal of Cellular Biochemistry·Pierre P ElenisteAngela Bruzzaniti
Oct 23, 2014·The Biochemical Journal·Santosh K VermaLeonid V Chernomordik
Jun 13, 2015·Journal of Bone and Mineral Metabolism·Gnanasagar J ThirukondaYasuhiro Kobayashi
Jan 7, 2014·The International Journal of Biochemistry & Cell Biology·Pierre P ElenisteAngela Bruzzaniti
Jun 21, 2020·Orthodontics & Craniofacial Research·Jun SunAngela Bruzzaniti

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