Structure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2.
Structure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2.
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DOI:
10.1016/j.str.2013.11.011
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发表时间:
2014-02-04
期刊:
影响因子:
5.7
通讯作者:
Rizo, Josep
中科院分区:
文献类型:
--
作者:
Xu, Junjie;Bacaj, Taulant;Zhou, Amy;Tomchick, Diana R.;Suedhof, Thomas C.;Rizo, Josep
Contacts between the endoplasmic reticulum and the plasma membrane involve extended synaptotagmins (E-Syts) in mammals or tricalbins in yeast, proteins with multiple C2 domains. One of the tandem C2 domains of E-Syt2 is predicted to bind Ca2+, but no Ca2+-dependent function has been attributed to this protein. We have determined the crystal structures of the tandem C2 domains of E-Syt2 in the absence and presence of Ca2+, and analyzed their Ca2+-binding properties by NMR spectroscopy. Our data reveal an unexpected V-shaped structure with a rigid orientation between the two C2 domains that is not substantially altered by Ca2+. The E-Syt2 C2A domain binds up to four Ca2+ ions, whereas the C2B domain does not bind Ca2+. These results suggest that E-Syt2 performs an as yet unidentified Ca2+-dependent function through its C2A domain, and uncover fundamental differences between the properties of the tandem C2 domains of E-Syts and synaptotagmins.
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