{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T22:02:21Z","timestamp":1790632941194,"version":"4.1.0"},"reference-count":36,"publisher":"The Company of Biologists","issue":"19","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2008,10,1]]},"abstract":"<jats:p>The stromal interacting molecule (STIM1) is pivotal for store-operated Ca2+ entry (SOC). STIM1 proteins sense the Ca2+ concentration within the lumen of the endoplasmic reticulum (ER) via an EF-hand domain. Dissociation of Ca2+ from this domain allows fast oligomerization of STIM1 and the formation of spatially discrete clusters close to the plasma membrane. By lifetime-imaging of STIM1 interaction, the rearrangement of STIM1, ER Ca2+ concentration ([Ca2+]ER) and cytosolic Ca2+ signals ([Ca2+]cyto) we show that [Ca2+]cyto affects the subcellular distribution of STIM1 oligomers and prevents subplasmalemmal STIM clustering, even if the ER is depleted. These data indicate that [Ca2+]cyto, independently of the ER Ca2+ filling state, crucially tunes the formation and disassembly of subplasmalemmal STIM1 clusters, and, thus, protects cells against Ca2+ overload resulting from excessive SOC activity.<\/jats:p>","DOI":"10.1242\/jcs.034496","type":"journal-article","created":{"date-parts":[[2008,9,3]],"date-time":"2008-09-03T00:55:00Z","timestamp":1220403300000},"page":"3133-3139","source":"Crossref","is-referenced-by-count":58,"title":["Cytosolic Ca2+ prevents the subplasmalemmal clustering of STIM1: an intrinsic mechanism to avoid Ca2+ overload"],"prefix":"10.1242","volume":"121","author":[{"given":"Roland","family":"Malli","sequence":"first","affiliation":[{"name":"Institute of Molecular Biology and Biochemistry, Center of Molecular Medicine, Medical University of Graz, Graz, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shamim","family":"Naghdi","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology and Biochemistry, Center of Molecular Medicine, Medical University of Graz, Graz, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christoph","family":"Romanin","sequence":"additional","affiliation":[{"name":"Institute of Biophysics, University of Linz, Linz, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang F.","family":"Graier","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology and Biochemistry, Center of Molecular Medicine, Medical University of Graz, Graz, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042520230357100_REF1","doi-asserted-by":"crossref","unstructured":"Bauer, M. 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