Journal
CELL
Volume 109, Issue 3, Pages 347-358Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(02)00708-0
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R01 GM038499, R01 GM038499-14] Funding Source: Medline
- PHS HHS [NIH 38499] Funding Source: Medline
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Unc104 (KIF1A) kinesin transports membrane vesicles along microtubules in lower and higher eukaryotes. Using an in vitro motility assay, we show that Unc104 uses a lipid binding pleckstrin homology (PH) domain to dock onto membrane cargo. Through its PH domain, Unc104 can transport phosphatidylinositol(4,5)bisphosphate (Ptdins(4,5)P-2)-containing liposomes with similar properties to native vesicles. Interestingly, liposome movement by monomeric Unc104 motors shows a very steep dependence on Ptdins(4,5)P-2 concentration (Hill coefficient of similar to20), even though liposome binding is noncooperative. This switch-like transition for movement can be shifted to lower Ptdins(4,5)P-2 concentrations by the addition of cholesterol/sphingomyelin or GM1 ganglioside/cholera toxin, conditions that produce raft-like behavior of Unc104 bound to lipid bilayers. These studies suggest that clustering of Unc104 in Ptdins(4,5)P-2-containing rafts provides a trigger for membrane transport.
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