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- 저자 : Bohbot, Hilla (검색결과 1 건)
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Lee, Su Youn,Giladi, Moshe,Bohbot, Hilla,Hiller, Reuben,Chung, Ka Young,Khananshvili, Daniel The Federation of American Societies for Experimen 2016 The FASEB Journal Vol.30 No.3
<P>Tissue-specific splice variants of Na+/Ca2+ exchangers contain 2 Ca2+-binding regulatory domains (CBDs), CBD1 and CBD2. Ca2+ interaction with CBD1 activates sodium-calcium exchangers (NCXs), and Ca2+ binding to CBD2 alleviates Na+-dependent inactivation. A combination of mutually exclusive (A, B) and cassette (C-F) exons in CBD2 raises functionally diverse splice variants through unknown mechanisms. Here, the effect of exons on CBDs backbone dynamics were investigated in the 2-domain tandem (CBD12) of the brain, kidney, and cardiac splice variants by using hydrogen-deuterium exchange mass spectrometry and stopped-flow techniques. Mutually exclusive exons stabilize interdomain interactions in the apoprotein, which primarily predefines the extent of responses to Ca2+ binding. Deuterium uptake levels were up to 20% lower in the cardiac vs. the brain CBD12, reveling that elongation of the CBD2 FG loop by cassette exons rigidifies the interdomain Ca2+ salt bridge at the 2-domain interface, which secondarily modulates the Ca2+-bound states. In matching splice variants, the extent of Ca2+-induced rigidification correlates with decreased (up to 10-fold) Ca2+ off rates, where the cardiac CBD12 exhibits the slowest Ca2+ off rates. Collectively, structurally disordered/dynamic segments at mutually exclusive and cassette exons have local and distant effects on the folded structures nearby the Ca2+ binding sites, which may serve as a structure-dynamic basis for splicing-dependent regulation of NCX.</P>
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