Asset Details
Do you wish to reserve the book?
lipid-anchored SNARE supports membrane fusion
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
lipid-anchored SNARE supports membrane fusion
Do you wish to request the book?
lipid-anchored SNARE supports membrane fusion
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
lipid-anchored SNARE supports membrane fusion
2011
Overview
Intracellular membrane fusion requires R-SNAREs and Q-SNAREs to assemble into a four-helical parallel coiled-coil, with their hydrophobic anchors spanning the two apposed membranes. Based on the fusion properties of chemically defined SNARE- proteoliposomes, it has been proposed that the assembly of this helical bundle transduces force through the entire bilayer via the transmembrane SNARE anchor domains to drive fusion. However, an R-SNARE, Nyv1p, with a genetically engineered lipid anchor that spans half of the bilayer suffices for the fusion of isolated vacuoles, although this organelle has other R-SNAREs. To demonstrate unequivocally the fusion activity of lipid-anchored Nyv1p, we reconstituted proteoliposomes with purified lipid-anchored Nyv1p as the only protein. When these proteoliposomes were incubated with those bearing cognate Q-SNAREs, there was trans-SNARE complex assembly but, in accord with prior studies of the neuronal SNAREs, little lipid mixing. However, the addition of physiological fusion accessory proteins (HOPS, Sec17p, and Sec18p) allows lipid-anchored Nyv1p to support fusion, suggesting that trans-SNARE complex function is not limited to force transduction across the bilayers through the transmembrane domains.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Lipid-Linked Proteins - chemistry
/ Lipid-Linked Proteins - physiology
/ Lipids
/ Membrane Fusion - physiology
/ Membrane Proteins - chemistry
/ Membrane Proteins - physiology
/ P branes
/ Proteins
/ Q-SNARE Proteins - chemistry
/ Q-SNARE Proteins - physiology
/ R-SNARE Proteins - chemistry
/ R-SNARE Proteins - physiology
/ Recombinant Proteins - chemistry
/ Saccharomyces cerevisiae - physiology
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - physiology
/ Vacuoles
/ Yeasts
