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First published online 3 May 2007
doi: 10.1242/jcs.03462

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New molecular players in capacitative Ca²⁺ entry

National Institute of Environmental Health Sciences – NIH, PO Box 12233, Research Triangle Park, NC 27709, USA

e-mail: putney{at}niehs.nih.gov

Accepted 19 April 2007

Capacitative Ca²⁺ entry links the emptying of intracellular Ca²⁺ stores to the activation of store-operated Ca²⁺ channels in the plasma membrane. In the twenty years since the inception of the concept of capacitative Ca²⁺ entry, a number of activation mechanisms have been proposed, and there has been considerable interest in the possibility that TRP channels function as store-operated channels. However, in the past two years, two major players in both the signaling and permeation mechanisms for store-operated channels have been discovered: Stim1 and the Orai proteins. Stim1 is an endoplasmic reticulum Ca²⁺ sensor. It appears to act by redistributing within a small component of the endoplasmic reticulum, approaching the plasma membrane, but does not seem to translocate into the plasma membrane. Stim1 signals to plasma membrane Orai proteins, which constitute pore-forming subunits of store-operated channels.

Key words: Store-operated Ca²⁺ entry, Ca²⁺ channels, Stim1, Orai1, Ca²⁺-release-activated Ca²⁺ current

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