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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.
Derler,
A Ca2(+ )release-activated Ca2(+) (CRAC) modulatory domain (CMD) within STIM1 mediates fast Ca2(+)-dependent inactivation of ORAI1 channels.
2009, Pubmed
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Pubmed Hogan,
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Pubmed Huang,
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Pubmed Kawasaki,
A minimal regulatory domain in the C terminus of STIM1 binds to and activates ORAI1 CRAC channels.
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Pubmed Lee,
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Pubmed Machaca,
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Xenbase Machaca,
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2000,
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Xenbase Muik,
A Cytosolic Homomerization and a Modulatory Domain within STIM1 C Terminus Determine Coupling to ORAI1 Channels.
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Pubmed Mullins,
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Pubmed Parekh,
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Pubmed Stathopulos,
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Pubmed Stathopulos,
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Pubmed Yeromin,
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Pubmed Yu,
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Xenbase Yu,
Orai1 internalization and STIM1 clustering inhibition modulate SOCE inactivation during meiosis.
2009,
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Xenbase Yuan,
SOAR and the polybasic STIM1 domains gate and regulate Orai channels.
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