Abstract
The p14 Fusion-associated Small Transmembrane (FAST) Protein Effects Membrane Fusion from a Subset of Membrane Microdomains
Highlights
Cholesterol depletion of donor cell membranes led to preferential disruption of p14 association with Lubrol WXresistant membranes and decreased cell-cell fusion activity, both of which were reversed upon subsequent cholesterol repletion
These data suggest that the p14 fusion-associated small transmembrane (FAST) protein associates with heterogeneous membrane microdomains, a distinct subset of which is defined by cholesterol-dependent Lubrol WX resistance and which may be more relevant to the membrane fusion process
Because the membrane environment from which the FAST proteins mediate the fusion reaction is the cell plasma membrane and in view of the potentially significant impact of the biophysical properties of plasma membrane lipid microdomains on models of the membrane fusion reaction, we determined whether this recently discovered novel family of membrane fusion proteins associates with membrane microdomains. Based on both detergent and nondetergent approaches, our results indicate that the p14 FAST protein associates with distinct membrane microdomains, a subset of which may contain p14 molecules more directly involved in the membrane fusion process
Summary
Follow this and additional works at: https://scholarworks.utrgv.edu/pa_fac Part of the Astrophysics and Astronomy Commons. Co-patching analysis by fluorescence microscopy indicated that p14 did not co-localize with classical lipidanchored raft markers These data suggest that the p14 FAST protein associates with heterogeneous membrane microdomains, a distinct subset of which is defined by cholesterol-dependent Lubrol WX resistance and which may be more relevant to the membrane fusion process. Because the membrane environment from which the FAST proteins mediate the fusion reaction is the cell plasma membrane and in view of the potentially significant impact of the biophysical properties of plasma membrane lipid microdomains on models of the membrane fusion reaction, we determined whether this recently discovered novel family of membrane fusion proteins associates with membrane microdomains Based on both detergent and nondetergent approaches, our results indicate that the p14 FAST protein associates with distinct membrane microdomains, a subset of which may contain p14 molecules more directly involved in the membrane fusion process
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