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J. Biol. Chem., Vol. 259, Issue 13, 8052-8055, 07, 1984
CJ Steer, JS Vincent and IW Levin
Clathrin, the major structural protein associated with both coated pits and
coated vesicles, has been implicated in the dynamics of various endocytotic
processes. In an attempt to define the mechanisms involved in the
transition from uncoated membranes to clathrin-coated pits and then to
coated vesicles, we investigated by infrared spectroscopy the lipid
perturbations arising from the interactions of the clathrin coat with the
bilayers of intact membrane assemblies. A comparison of the lipid acyl
chain symmetric methylene stretching modes at approximately 2850 cm-1 for
isolated clathrin-coated vesicles, uncoated vesicles, and synaptic
membranes at 21, 38, and 50 degrees C indicated that clathrin significantly
increases the number of gauche chain conformers in the bilayer matrix of
the coated vesicle system. The increase in lipid disorder at 21 degrees C,
accompanying the observed 0.44-cm-1 frequency increase for coated vesicles
compared to uncoated vesicles, is approximately equivalent to the
intrachain disorder incurred in heating liquid crystalline
dimyristoylphosphatidylcholine multilayers by approximately 10 degrees C.
The implications of these results on coated vesicle formation are
discussed.
Membrane lipid response to clathrin coat protein determined by infrared spectroscopy. Possible involvement in coated vesicle formation
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