title: Membrane lipids influence protein complex assembly-disassembly.
abstract: Approximately 11% smaller t-/v-SNARE ring complexes are generated using 50 nm cholesterol-associated vesicles as opposed to vesicles containing L-alpha-lysophosphatidylcholine (LPC), as observed using atomic force microscopy. Circular dichroism spectroscopy demonstrated that in the presence of LPC as opposed to cholesterol, N-ethylmaleimide-sensitive factor + adenosine triphosphate induces disassembly of beta-sheet structures but not the alpha-helical contents within the t-/v-SNARE complex.
authors.affiliation: Department of Physiology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
authors.forename: Leah
authors.initials: L
authors.lastname: Shin
authors.forename: Won Jin
authors.initials: WJ
authors.lastname: Cho
authors.forename: Jeremy D
authors.initials: JD
authors.lastname: Cook
authors.forename: Timothy L
authors.initials: TL
authors.lastname: Stemmler
authors.forename: Bhanu P
authors.initials: BP
authors.lastname: Jena
mesh_terms: D002784:Cholesterol / Q000378:metabolism; D002942:Circular Dichroism; D008244:Lysophosphatidylcholines / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D011485:Protein Binding; D017433:Protein Structure, Secondary; D050600:SNARE Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D008244:Lysophosphatidylcholines; D008563:Membrane Lipids; D050600:SNARE Proteins; D002784:Cholesterol