The carboxy-terminal domain of complexin I stimulates liposome fusion

被引:51
作者
Malsam, Joerg [1 ]
Seiler, Florian [1 ]
Schollmeier, Yvette [1 ]
Rusu, Patricia [1 ]
Krause, Jean Michel [1 ]
Soellner, Thomas H. [1 ]
机构
[1] Univ Heidelberg, Biochem Ctr, D-69120 Heidelberg, Germany
基金
美国国家卫生研究院;
关键词
exocytosis; SNARE; SYNAPTIC VESICLE EXOCYTOSIS; NEUROTRANSMITTER RELEASE; SNARE COMPLEX; MEMBRANE-FUSION; PHOSPHOLIPID-VESICLES; DISTINCT DOMAINS; SYNAPTOTAGMIN; BINDING; PROTEIN; CA2+;
D O I
10.1073/pnas.0812813106
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Regulated exocytosis requires tight coupling of the membrane fusion machinery to a triggering signal and a fast response time. Complexins are part of this regulation and, together with synaptotagmins, control calcium-dependent exocytosis. Stimulatory and inhibitory functions have been reported for complexins. To test if complexins directly affect membrane fusion, we analyzed the 4 known mammalian complexin isoforms in a reconstituted fusion assay. In contrast to complexin III (CpxIII) and CpxIV, CpxI and CpxII stimulated soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-pin assembly and membrane fusion. This stimulatory effect required a preincubation at low temperature and was specific for neuronal t-SNAREs. Stimulation of membrane fusion was lost when the carboxy-terminal domain of CpxI was deleted or serine 115, a putative phosphorylation site, was mutated. Transfer of the carboxy-terminal domain of CpxI to CpxIII resulted in a stimulatory CpxIII-I chimera. Thus, the carboxyterminal domains of CpxI and CpxII promote the fusion of high-curvature liposomes.
引用
收藏
页码:2001 / 2006
页数:6
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