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Molecular Biology of the Cell|September 6, 2023
MARCKS Effector Domain, a reversible lipid ligand, illuminates late stages of membrane fusionAmy Orr, William WicknerThe Journal of Biological Chemistry|August 6, 2009
Complex lipid requirements for SNARE- and SNARE chaperone-dependent membrane fusionJoji Mima, William WicknerMolecular Biology of the Cell|September 8, 2021
Phosphatidylinositol and phosphatidylinositol-3-phosphate activate HOPS to catalyze SNARE assembly, allowing small headgroup lipids to support the terminal steps of membrane fusionThomas Torng, William WicknerThe Journal of Cell Biology|September 27, 2006
Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeastChao-Wen Wang, Susan Hamamoto, Lelio Orci, et al.Proceedings of the National Academy of Sciences of the United States of America|June 26, 2019
Tethering guides fusion-competent trans-SNARE assemblyHongki Song, William WicknerProceedings of the National Academy of Sciences of the United States of America|October 7, 2009
Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusionJoji Mima, William WicknerThe Journal of Biological Chemistry|August 20, 2013
Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7pVidya Karunakaran, William WicknerProceedings of the National Academy of Sciences of the United States of America|November 6, 2019
Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartmentsYoungsoo Jun, William WicknerMolecular Biology of the Cell|March 16, 2017
A cascade of multiple proteins and lipids catalyzes membrane fusionWilliam Wickner, Josep RizoMolecular Biology of the Cell|March 27, 2024
Sec18 binds the tethering/SM complex HOPS to engage the Qc-SNARE for membrane fusionAmy Orr, William WicknerPageof 18