Phosphorylation of STIM1 at ERK/CDK sites is dispensable for cell migration and ER partitioning in mitosis
<p dir="ltr">Store-operated Ca<sup>2+</sup> entry (SOCE) is a ubiquitous Ca<sup>2+</sup> influx pathway required for multiple physiological functions including cell motility. SOCE is triggered in response to depletion of intracellular Ca<sup>2+</sup&g...
محفوظ في:
| المؤلف الرئيسي: | |
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| مؤلفون آخرون: | , , , , |
| منشور في: |
2021
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| الموضوعات: | |
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| الملخص: | <p dir="ltr">Store-operated Ca<sup>2+</sup> entry (SOCE) is a ubiquitous Ca<sup>2+</sup> influx pathway required for multiple physiological functions including cell motility. SOCE is triggered in response to depletion of intracellular Ca<sup>2+</sup> stores following the activation of the endoplasmic reticulum (ER) Ca<sup>2+</sup> sensor STIM1, which recruits the plasma membrane (PM) Ca<sup>2+</sup> 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.</p><h2>Other Information</h2><p dir="ltr">Published in: Cell Calcium<br>License: <a href="http://creativecommons.org/licenses/by/4.0/" target="_blank">http://creativecommons.org/licenses/by/4.0/</a><br>See article on publisher's website: <a href="https://dx.doi.org/10.1016/j.ceca.2021.102496" target="_blank">https://dx.doi.org/10.1016/j.ceca.2021.102496</a></p> |
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