SPAK and OSR1 kinases bind and phosphorylate the β2-Adrenergic receptor

Elzwawi, Abdulrahman, Grafton, Gillian, Barnes, Nicholas M. and Mehellou, Youcef ORCID: https://orcid.org/0000-0001-5720-8513 2020. SPAK and OSR1 kinases bind and phosphorylate the β2-Adrenergic receptor. Biochemical and Biophysical Research Communications 532 (1) , pp. 88-93. 10.1016/j.bbrc.2020.07.143

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Abstract

SPAK and OSR1 are two cytoplasmic serine/threonine protein kinases that regulate the function of a series of sodium, potassium and chloride co-transporters via phosphorylation. Over recent years, it has emerged that these two kinases may have diverse function beyond the regulation of ion co-transporters. Inspired by this, we explored whether SPAK and OSR1 kinases impact physically and phosphorylate the β2-adrenergic receptor (β2ADR). Herein, we report that the amino acid sequence of the human β2ADR displays a SPAK/OSR1 consensus binding motif and using a series of pulldown and in vitro kinase assays we show that SPAK and OSR1 bind the β2ADR and phosphorylate it in vitro. This work provides a notable example of SPAK and OSR1 kinases binding to a G-protein coupled receptor and taps into the potential of these protein kinases in regulating membrane receptors beyond ion co-transporters.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Pharmacy
Publisher:	Elsevier
ISSN:	0006-291X
Date of First Compliant Deposit:	8 September 2020
Date of Acceptance:	31 July 2020
Last Modified:	04 Dec 2024 08:00
URI:	https://orca.cardiff.ac.uk/id/eprint/134725

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