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

Abdulrahman Elzwawi, Gillian Grafton, Nicholas Barnes, Youcef Mehellou

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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.
Original languageEnglish
Pages (from-to)88-93
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Early online date20 Aug 2020
Publication statusPublished - 29 Oct 2020


  • Binding
  • OSR1
  • Phosphorylation
  • SPAK
  • β2ADR


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