Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism
- Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism
- 민두영; 김기범; 현창봉; 조용훈; 신년균; 윤태영
- Biological sciences; Biophysics; Cell biology
- Issue Date
- Nature Communications
- VOL 4, 1705-1-1705-10
- Formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex provides mechanical thrust for membrane fusion, but its molecular mechanism is still unclear. Here using magnetic tweezers, we observe mechanical responses of a single neuronal SNARE complex under constant pulling force. Single SNARE complexes may be unzipped with 34 pN force. When rezipping is induced by lowering the force to 11 pN, only a partially assembled state results, with the C-terminal half of the SNARE complex remaining disassembled. Reassembly of the C-terminal half occurs only when the force is further lowered below 11 pN. Thus, mechanical hysteresis, characterized by the unzipping and rezipping cycle of a single SNARE complex, produces the partially assembled state. In this metastable state, unzipping toward the N-terminus is suppressed while zippering toward the C-terminus is initiated as a steep function of force. This ensures the directionality of SNARE-complex formation, making the SNARE complex a robust force-generating machine.
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