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Complexin cross-links prefusion SNAREs into a zigzag array
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Complexin cross-links prefusion SNAREs into a zigzag array
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Journal Article
Complexin cross-links prefusion SNAREs into a zigzag array
2011
Overview
Structural studies of complexin bound to a mimetic of a prefusion SNARE complex provide insight into how complexin 'clamps' SNARE complex assembly, thereby inhibiting membrane fusion. While the central helix of complexin is anchored to a SNARE complex, its accessory helix extends away and bridges to a second SNARE complex, generating a zigzag array incompatible with fusion.
Complexin prevents SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. To understand the mechanism for this inhibition, we determined the structure of complexin bound to a mimetic of a prefusion SNAREpin lacking the portion of the v-SNARE that zippers last to trigger fusion. The 'central helix' of complexin is anchored to one SNARE complex, while its 'accessory helix' extends away at ~45° and bridges to a second complex, occupying the vacant v-SNARE binding site to inhibit fusion. We expected the accessory helix to compete with the v-SNARE for t-SNARE binding but found instead that the interaction occurs intermolecularly. Thus, complexin organizes the SNAREs into a zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Adaptor Proteins, Vesicular Transport - chemistry
/ Adaptor Proteins, Vesicular Transport - metabolism
/ Adaptor Proteins, Vesicular Transport - physiology
/ Animals
/ Biomedical and Life Sciences
/ Humans
/ Lipids
/ Membrane Fusion - physiology
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - metabolism
/ Nerve Tissue Proteins - physiology
/ Proteins
/ Rats
/ Topology
/ Vesicle-Associated Membrane Protein 2 - chemistry
