title: Membrane fusion: SNAREs and regulation.
abstract: SNARE (SNAP receptor) proteins drive intracellular membrane fusion and contribute specificity to membrane trafficking. The formation of SNAREpins between membranes is spatially and temporally controlled by a network of sequentially acting accessory components. These regulators add an additional layer of specificity, arrest SNAREpin intermediates, lower the energy required for fusion, and couple membrane fusion to triggering signals. The functional activity of some of these regulators determines the plasticity of regulated exocytosis.
authors: Biochemistry Center, University Heidelberg, Im Neuenheimer Feld 345, 69120 Heidelberg, Germany.
authors: J
authors: J
authors: Malsam
authors: S
authors: S
authors: Kreye
authors: T H
authors: TH
authors: Söllner
mesh_terms: D000818:Animals; D005089:Exocytosis / Q000502:physiology; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology*; D051938:Munc18 Proteins / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism; D050682:Q-SNARE Proteins / Q000378:metabolism; D050683:R-SNARE Proteins / Q000378:metabolism; D050600:SNARE Proteins / Q000737:chemistry / Q000378:metabolism*; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins / Q000378:metabolism; D050857:Synaptotagmins / Q000378:metabolism; D022161:Transport Vesicles / Q000378:metabolism
chemical_list: D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins; D050682:Q-SNARE Proteins; D050683:R-SNARE Proteins; D050600:SNARE Proteins; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D050857:Synaptotagmins