ArticleThe Journal of biological chemistry2011
Role of the STIM1 C-terminal domain in STIM1 clustering.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- The carboxy terminal coiled-coil modulates Orai1 internalization during meiosis.Scientific reports · 2021Article
- Cross-talk between N-terminal and C-terminal domains in stromal interaction molecule 2 (STIM2) determines enhanced STIM2 sensitivity.The Journal of biological chemistry · 2019Article
- Sequential Steps of CRAC Channel Activation.Cell reports · 2017Article
- STIM1 Phosphorylation at Y361 Recruits Orai1 to STIM1 Puncta and Induces CaScientific reports · 2017Article
- Cooperative Binding of Stromal Interaction Molecule 1 (STIM1) to the N and C Termini of Calcium Release-activated Calcium Modulator 1 (Orai1).The Journal of biological chemistry · 2016Article
- Xenopus Oocyte As a Model System to Study Store-Operated Ca(2+) Entry (SOCE).Frontiers in cell and developmental biology · 2016Article
- Critical role for Orai1 C-terminal domain and TM4 in CRAC channel gating.Cell research · 2015Article
- STIM proteins: dynamic calcium signal transducers.Nature reviews. Molecular cell biology · 2012Review
- Structural and mechanistic insights into the activation of Stromal interaction molecule 1 (STIM1).Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Regulation of store-operated calcium entry during cell division.Biochemical Society transactions · 2012Article
- Unlocking SOAR releases STIM.The EMBO journal · 2011Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Store-operated Ca(2+) entry (SOCE) represents a ubiquitous Ca(2+) influx pathway activated by the filling state of intracellular Ca(2+) stores. SOCE is mediated by coupling of STIM1, the endoplasmic reticulum Ca(2+) sensor, to the Orai1 channel. SOCE inactivates during meiosis, partly because of the inability of STIM1 to cluster in response to store depletion. STIM1 has several functional domains, including the Orai1 interaction domain (STIM1 Orai Activating Region (SOAR) or CRAC Activation Domain (CAD)) and STIM1 homomerization domain. When Ca(2+) stores are full, these domains are inactive to prevent constitutive Ca(2+) entry. Here we show, using the Xenopus oocyte as an expression system, that the C-terminal 200 residues of STIM1 are important to maintain STIM1 in an inactive state when Ca(2+) stores are full, through predicted intramolecular shielding of the active STIM1 domains (SOAR/CAD and STIM1 homomerization domain). Interestingly, our data argue that the C-terminal 200 residues accomplish this through a steric hindrance mechanism because they can be substituted by GFP or mCherry while maintaining all aspects of STIM1 function. We further show that STIM1 clustering inhibition during meiosis is independent of the C-terminal 200 residues.
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