Membrane lipids influence protein complex assembly-disassembly.
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.
Shin
Leah
L
Department of Physiology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
Cho
Won Jin
WJ
Cook
Jeremy D
JD
Stemmler
Timothy L
TL
Jena
Bhanu P
BP
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*
D008244:Lysophosphatidylcholines; D008563:Membrane Lipids; D050600:SNARE Proteins; D002784:Cholesterol