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Malli, R; Naghdi, S; Romanin, C; Graier, WF.
Cytosolic Ca2+ prevents the subplasmalemmal clustering of STIM1: an intrinsic mechanism to avoid Ca2+ overload.
J Cell Sci. 2008; 121(Pt 19): 3133-3139. [OPEN ACCESS]
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Autor/innen der Med Uni Graz:
Graier Wolfgang
Malli Roland
Naghdi Shamim

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Number of Figures: 4
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The stromal interacting molecule (STIM1) is pivotal for store-operated Ca(2+) entry (SOC). STIM1 proteins sense the Ca(2+) concentration within the lumen of the endoplasmic reticulum (ER) via an EF-hand domain. Dissociation of Ca(2+) 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 Ca(2+) concentration ([Ca(2+)](ER)) and cytosolic Ca(2+) signals ([Ca(2+)](cyto)) we show that [Ca(2+)](cyto) affects the subcellular distribution of STIM1 oligomers and prevents subplasmalemmal STIM clustering, even if the ER is depleted. These data indicate that [Ca(2+)](cyto), independently of the ER Ca(2+) filling state, crucially tunes the formation and disassembly of subplasmalemmal STIM1 clusters, and, thus, protects cells against Ca(2+) overload resulting from excessive SOC activity.
Find related publications in this database (using NLM MeSH Indexing)
Calcium - metabolism
Cell Line -
Cell Membrane - drug effects
Cytosol - drug effects
Egtazic Acid - analogs and derivatives
Endoplasmic Reticulum - drug effects
Histamine - pharmacology
Humans -
Membrane Proteins - chemistry
Protein Multimerization - drug effects
Thermodynamics -

Find related publications in this database (Keywords)
ER Ca2+ dynamics
STIM1 oligomerization
store-operated Ca2+ entry
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