Sealed with a twist: complexin and the synaptic SNARE complex.
Knockout experiments show that complexins are crucial for Ca(2+)-dependent neurotransmitter release. In the recently solved crystal structure of complexin I bound to the synaptic SNARE complex, complexin binds along the groove between the syntaxin and synaptobrevin coils. This structure, together with NMR data, suggests that the role of complexin is to stabilize the SNARE complex as it forms from SNAREs in vesicle and target membranes.
Department of Cell Biology and Physiology, Washington University School of Medicine, 660 South Euclid Avenue, Box 8228, St Louis, MO 6311, USA.
Karla E
KE
Marz
Phyllis I
PI
Hanson
D033942:Adaptor Proteins, Vesicular Transport; D000818:Animals; D001921:Brain / Q000166:cytology / Q000378:metabolism*; D020013:Calcium Signaling / Q000502:physiology; D005089:Exocytosis / Q000502:physiology*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D017729:Presynaptic Terminals / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology; D050600:SNARE Proteins; D013570:Synaptic Membranes / Q000378:metabolism* / Q000648:ultrastructure; D009435:Synaptic Transmission / Q000502:physiology*; D033921:Vesicular Transport Proteins
D033942:Adaptor Proteins, Vesicular Transport; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins; C095992:complexin I