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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The short N-terminal domains of STIM1 and STIM2 control the activation kinetics of Orai1 channels.

STIM1 and STIM2 are dynamic transmembrane endoplasmic reticulum Ca(2+) sensors, coupling directly to activate plasma membrane Orai Ca(2+) entry channels. Despite extensive sequence homology, the STIM proteins are functionally distinct. We reveal that the short variable N-terminal random coil sequences of STIM1 and STIM2 confer profoundly different activation properties. Using Orai1-expressing HEK293 cells, chimeric replacement of the 43-amino-acid STIM1 N terminus with that of STIM2 attenuates Orai1-mediated Ca(2+) entry and drastically slows store-induced Orai1 channel activation. Conversely, the 55-amino-acid STIM2 terminus substituted within STIM1 strikingly enhances both Orai1-mediated Ca(2+) entry and constitutive coupling to activate Orai1 channels. Hence, STIM N termini are powerful coupling modifiers, functioning in STIM2 to "brake" the otherwise constitutive activation of Orai1 channels afforded by its high sensitivity to luminal Ca(2+).[1]


  1. The short N-terminal domains of STIM1 and STIM2 control the activation kinetics of Orai1 channels. Zhou, Y., Mancarella, S., Wang, Y., Yue, C., Ritchie, M., Gill, D.L., Soboloff, J. J. Biol. Chem. (2009) [Pubmed]
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