NDLI: STIM1 dimers undergo unimolecular coupling to activate Orai1 channels

Content Provider	PubMed Central
Author	Zhou, Yandong Wang, Xizhuo Wang, Xianming Loktionova, Natalia A. Cai, Xiangyu Nwokonko, Robert M. Vrana, Erin Wang, Youjun Rothberg, Brad S. Gill, Donald L.
Copyright Year	2015
Abstract	The endoplasmic reticulum (ER) Ca2+ sensor, STIM1, becomes activated when ER-stored Ca2+ is depleted and translocates into ER–plasma membrane junctions where it tethers and activates Orai1 Ca2+ entry channels. The dimeric STIM1 protein contains a small STIM-Orai-activating region (SOAR)—the minimal sequence sufficient to activate Orai1 channels. Since SOAR itself is a dimer, we constructed SOAR concatemer–dimers and introduced mutations at F394, which is critical for Orai1 coupling and activation. The F394H mutation in both SOAR monomers completely blocks dimer function, but F394H introduced in only one of the dimeric SOAR monomers has no effect on Orai1 binding or activation. This reveals an unexpected unimolecular coupling between STIM1 and Orai1 and argues against recent evidence suggesting dimeric interaction between STIM1 and two adjacent Orai1 channel subunits. The model predicts that STIM1 dimers may be involved in crosslinking between Orai1 channels with implications for the kinetics and localization of Orai1 channel opening.
Related Links	http://dx.doi.org/10.1038/ncomms9395
Starting Page	8395
File Format	PDF
ISSN	20411723
e-ISSN	20411723
Journal	Nature Communications
Volume Number	6
Language	English
Publisher	Nature Pub. Group
Publisher Date	2015-09-01
Access Restriction	Open
Rights Holder	Nature Pub. Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Physics and Astronomy(all) Chemistry(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry Physics and Astronomy Biochemistry, Genetics and Molecular Biology

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STIM1 dimers undergo unimolecular coupling to activate Orai1 channels

STIM1 dimers undergo unimolecular coupling to activate Orai1 channels

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STIM1 triggers a gating rearrangement at the extracellular mouth of the ORAI1 channel

STIM1 Clusters and Activates CRAC Channels via Direct Binding of a Cytosolic Domain to Orai1

Distinct Orai-coupling domains in STIM1 and STIM2 define the Orai-activating site

Translocation between PI(4,5)P2-poor and PI(4,5)P2-rich microdomains during store depletion determines STIM1 conformation and Orai1 gating

A Cytosolic Homomerization and a Modulatory Domain within STIM1 C Terminus Determine Coupling to ORAI1 Channels* S⃞

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STIM1 dimers undergo unimolecular coupling to activate Orai1 channels

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STIM1 dimers undergo unimolecular coupling to activate Orai1 channels

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STIM1 triggers a gating rearrangement at the extracellular mouth of the ORAI1 channel

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Translocation between PI(4,5)P2-poor and PI(4,5)P2-rich microdomains during store depletion determines STIM1 conformation and Orai1 gating

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