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JCS ePress online publication date 9 Oct 2007
doi: 10.1242/jcs.015735

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Research Article

Role of the microtubule cytoskeleton in the function of the store-operated Ca2+ channel activator STIM1


Jeremy T. Smyth, Wayne I. DeHaven, Gary S. Bird, and James W. Putney Jr*
* Author for correspondence (e-mail: putney{at}niehs.nih.gov)

We examined the role of the microtubule cytoskeleton in the localization and store-operated Ca2+ entry (SOCE) function of the endoplasmic reticulum (ER) Ca2+ sensor stromal interaction molecule 1 (STIM1) in HEK 293 cells. STIM1 tagged with an enhanced yellow fluorescent protein (EYFP-STIM1) exhibited a fibrillar localization that colocalized with endogenous {alpha}-tubulin. Depolymerization of microtubules with nocodazole caused a change from a fibrillar EYFP-STIM1 localization to one that was similar to that of the ER. Treatment of HEK 293 cells with nocodazole had a detrimental impact on SOCE and the associated Ca2+ release-activated Ca2+ current (ICRAC). This inhibition was significantly reversed in cells overexpressing EYFP-STIM1, implying that the primary inhibitory effect of nocodazole is related to STIM1 function. Surprisingly, nocodazole treatment alone induced significant SOCE and ICRAC in cells expressing EYFP-STIM1, and this was accompanied by an increase in EYFP-STIM1 fluorescence near the plasma membrane. We conclude that microtubules play a facilitative role in the SOCE signaling pathway by optimizing the localization of STIM1.




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