TAILIEUCHUNG - Báo cáo khoa học: A single EF-hand isolated from STIM1 forms dimer in the absence and presence of Ca2+

Stromal interaction molecule 1 (STIM1) is responsible for activating the Ca 2+ release-activated Ca 2+ (CRAC) channel by first sensing the changes in Ca 2+ concentration in the endoplasmic reticulum ([Ca 2+ ]ER) via its luminal canonical EF-hand motif and subsequently oligomerizing to inter-act with the CRAC channel pore-forming subunit Orai1. | ỊFEBS Journal A single EF-hand isolated from STIM1 forms dimer in the absence and presence of Ca2 Yun Huang Yubin Zhou Hing-Cheung Wong Yanyi Chen Yan Chen Siming Wang Adriana Castiblanco Aimin Liu and Jenny J. Yang Department of Chemistry Center for Drug Design and Advanced Biotechnology Georgia State University Atlanta GA USA Keywords affinity Ca2 EF-hand oligomerization STIM1 Correspondence J. J. Yang Department of Chemistry Georgia State University Atlanta GA 30303 USA Fax 1 404 413 5551 Tel 1 404 413 5520 E-mail chejjy@ Received 21 March 2009 revised 26 June 2009 accepted 27 July 2009 doi Stromal interaction molecule 1 STIM1 is responsible for activating the Ca2 release-activated Ca2 CRAC channel by first sensing the changes in Ca2 concentration in the endoplasmic reticulum Ca2 ER via its luminal canonical EF-hand motif and subsequently oligomerizing to interact with the CRAC channel pore-forming subunit Orai1. In this work we applied a grafting approach to obtain the intrinsic metal-binding affinity of the isolated EF-hand of STIM1 and further investigated its oligomeric state using pulsed-field gradient NMR and size-exclusion chromatography. The canonical EF-hand bound Ca2 with a dissociation constant at a level comparable with Ca2 ER 512 15 pM . The binding of Ca2 resulted in a more compact conformation of the engineered protein. Our results also showed that D to A mutations at Ca2 -coordinating loop positions 1 and 3 of the EF-hand from STIM1 led to a 15-fold decrease in the metalbinding affinity which explains why this mutant was insensitive to changes in Ca2 concentration in the endoplasmic reticulum Ca2 ER and resulted in constitutive punctae formation and Ca2 influx. In addition the grafted single EF-hand motif formed a dimer regardless of the presence of Ca2 which conforms to the EF-hand paring paradigm. These data indicate that the STIM1 canonical EF-hand motif tends to dimerize for functionality in .

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