Complexin is able to bind to SNARE core complexes in different assembled states with distinct affinity |
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Authors: | Liu Jingguo Guo Ting Wei Yong Liu Ming Sui Sen-Fang |
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Affiliation: | Department of Biological Sciences and Biotechnology, State-Key Laboratory of Biomembrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China |
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Abstract: | The formation of the functional SNARE complex in vivo is central to the fast neurotransmitter release at the neuronal terminal. Numerous studies revealed that this process involves progressive assembly of an α-helical bundle and is dynamically reversible. So far many proteins directly or indirectly take part in this process. Complexin, one of such factors, has revealed rapid association with the SNARE complex, however, whether or not complexin can interact with partially assembled SNARE complex is critical and yet unknown. Here, we present evidence that complexin is able to bind to various mutant versions of the SNARE complex mimicking its quaternary structure at different assembly stages. In addition, the affinity of complexin for the SNARE complex is correlated with the extent to which the SNARE complex is assembled. These results suggest that complexin is able to bind to SNARE complex before its complete formation. |
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Keywords: | SNARE complex Complexin Interaction Membrane fusion Half-zippering |
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