Mapping interactions between the CRAC activation domain and CC1 regulating the activity of the ER Ca2+ sensor STIM1
Nisha Shrestha(Northwestern University), Ann Hye-Ryong Shim(Northwestern University), Mohammad Mehdi Maneshi(Northwestern University), Priscilla S.-W. Yeung(Northwestern University), Megumi Yamashita(Northwestern University), Murali Prakriya(Northwestern University)
Cited by 17Open Access
Abstract
stores. By contrast, altering the hydrophobic residues L265 and L273 strengthens the clamp to prevent STIM1 activation. Inclusion of the inactivation domain of STIM1 helps stabilize CC1-CAD interaction in several mutants to prevent spontaneous STIM1 activation. In addition, R426C, a human disease-linked mutation in CC3, affects the clamp but also impairs Orai1 binding to inhibit CRAC channel activation. These results identify the CC2, apex, and inactivation domain regions of STIM1 as important determinants of STIM1 activation.
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