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Park, Chan Young
Calcium Dynamics Lab
Research Interests
  • Calcium Signaling, Calcium Channels, Immune, neuroscience, Drug Development, Virus and host cell interaction.

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

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Title
STIM1 Clusters and Activates CRAC Channels via Direct Binding of a Cytosolic Domain to Orai1
Author
Park, Chan YoungHoover, Paul J.Mullins, Franklin M.Bachhawat, PritiCovington, Elizabeth D.Raunser, StefanWalz, ThomasGarcia, K. ChristopherDolmetsch, Ricardo E.Lewis, Richard S.
Issue Date
2009-03
Publisher
CELL PRESS
Citation
CELL, v.136, no.5, pp.876 - 890
Abstract
Store-operated Ca2+ channels activated by the depletion of Ca2+ from the endoplasmic reticulum (ER) are a major Ca2+ entry pathway in nonexcitable cells and are essential for T cell activation and adaptive immunity. After store depletion, the ER Ca2+ sensor STIM1 and the CRAC channel protein Orai1 redistribute to ER-plasma membrane (PM) junctions, but the fundamental issue of how STIM1 activates the CRAC channel at these sites is unresolved. Here, we identify a minimal, highly conserved 107-aa CRAC activation domain (CAD) of STIM1 that binds directly to the N and C termini of Orai1 to open the CRAC channel. Purified CAD forms a tetramer that clusters CRAC channels, but analysis of STIM1 mutants reveals that channel clustering is not sufficient for channel activation. These studies establish a molecular mechanism for store-operated Ca2+ entry in which the direct binding of STIM1 to Orai1 drives the accumulation and the activation of CRAC channels at ER-PM junctions.
URI
https://scholarworks.unist.ac.kr/handle/201301/7172
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=61349137530
DOI
10.1016/j.cell.2009.02.014
ISSN
0092-8674
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BIO_Journal Papers
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