NSF is important in vesicular trafficking, but neural expression of a dominant negative form of NSF2 induces an unexpected overgrowth of the DRosophila larval neuromuscular synapse
Pex1p possesses two distinct oligomeric forms, a homo-oligomer in the cytosol and a hetero-oligomer on peroxisome membranes, possibly playing distinct functions in peroxisome biogenesis
N-ethylmaleimide-sensitive factor is required for the synaptic incorporation and removal of 2-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors during cerebellar long-term depression
the enzyme plays a crucial role in the fusion of vesicles with target membranes. NSF-SNAP complexes may be involved in the disassembly of coiled-coil-mediated interactions underlying not only SNARE complexes but also other forms of stable oligomers, and the C-terminal membrane anchoring of NSF-SNAP targets may be mechanistically involved in the dissociation process
Vps4 disassembles the ESCRT-III protein polymer, thereby changing the morphology of the underlying membrane. The disassembly reaction causes the ESCRT-III subunits to regain the monomeric conformational state, which is the high-energy state that is poised to reassemble again into the ESCRT-III oligomer for subsequent rounds of membrane scission. When assembled, Vps4 progresses through many ATP hydrolysis cycles without dissociation
modeling of NSF-mediated disassembly in which the reaction is initiated by a 1:1 interaction between alpha-SNAP and the ternary SNARE complex, followed by NSF binding. Subsequent additional alpha-SNAP binding events may occur as part of a processive disassembly mechanism
residues from helix 5 of the Vps2p subunit of ESCRT-III bind to the central pore of an asymmetric Vps4p hexamer in a manner that is dependent upon the presence of flexible nucleotide analogues that can mimic multiple states in the ATP hydrolysis cycle, quantitative binding studies. Vps2p helix 5 peptides bind the Vps4p ATPase cassette. Vps4 substrates are initially recruited by an MIM-MIT interaction that activates the Vps4 central pore to engage substrates and generate force, thereby triggering ESCRT-III disassembly. The Vps4p hexamer binds a single peptide