STIM1 tyrosine-phosphorylation is required for STIM1-Orai1 association in human platelets

Esther Lopez, Isaac Jardin, Alejandro Berna-Erro, Nuria Bermejo, Ginés M. Salido, Stewart O. Sage, Juan A. Rosado, Pedro C. Redondo
  • Cellular Signalling, June 2012, Elsevier
  • DOI: 10.1016/j.cellsig.2012.02.012

What is it about?

Stromal interaction molecule 1 (STIM1) is a key element of the store-operated Ca2+ entry mechanism (SOCE). Recently, regulation of STIM1 by glycosylation and phosphorylation on serine/threonine or proline residues has been described; however other modes of phosphorylation that are important for activating SOCE in platelets, such as tyrosine phosphorylation, have been poorly investigated. Here we investigate the latency of STIM1 phosphorylation on tyrosine residues during the first steps of SOCE activation.

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The following have contributed to this page: Dr Nuria Bermejo