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Phosphorylation of STIM1 at ERK/CDK sites is dispensable for cell migration and ER partitioning in mitosis

journal contribution
submitted on 2023-10-18, 09:10 and posted on 2023-10-18, 11:59 authored by Ayat S. Hammad, Fang Yu, Welathanthrige S. Botheju, Asha Elmi, Ethel Alcantara-Adap, Khaled Machaca

Store-operated Ca2+ entry (SOCE) is a ubiquitous Ca2+ influx pathway required for multiple physiological functions including cell motility. SOCE is triggered in response to depletion of intracellular Ca2+ stores following the activation of the endoplasmic reticulum (ER) Ca2+ sensor STIM1, which recruits the plasma membrane (PM) Ca2+ channel Orai1 at ER-PM junctions. STIM1 is phosphorylated dynamically, and this phosphorylation has been implicated in several processes including SOCE inactivation during M-phase, maximal SOCE activation, ER segregation during mitosis, and cell migration. Human STIM1 has 10 Ser/Thr residues in its cytosolic domain that match the ERK/CDK consensus phosphorylation. We recently generated a mouse knock-in line where wild-type STIM1 was replaced by a non-phosphorylatable STIM1 with all ten S/Ts mutated to Ala (STIM1–10A). Here, we generate mouse embryonic fibroblasts (MEF) from the STIM1–10A mouse line and a control MEF line (WT) that express wild-type STIM1 from a congenic mouse strain. These lines offer a unique model to address the role of STIM1 phosphorylation at endogenous expression levels in contrast to previous studies that relied mostly on overexpression. We show that STIM1 phosphorylation at ERK/CDK sites is not required for SOCE activation, cell migration, or ER partitioning during mitosis. These results rule out STIM1 phosphorylation as a regulator of SOCE, migration, and ER distribution in mitosis.

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Published in: Cell Calcium
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  • English



Publication Year

  • 2021

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This Item is licensed under the Creative Commons Attribution 4.0 International License

Institution affiliated with

  • Weill Cornell Medicine - Qatar
  • Hamad Bin Khalifa University
  • College of Health and Life Sciences - HBKU

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