Brain clathrin complex: II. Immunofluorescent correlation and biochemical affinity for actin.

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Abstract
The interaction of [bovine] clathrin with cytoskeletal proteins was studied cytochemically by immunofluorescent staining and biochemically by the binding of actin to clathrin on the surfaces of polystyrene particles. Using a cytoskeletal-disrupting agent, the linear arrangement of clathrin lattices along actin fibers was altered. As a result of cell retraction, the flourescent dots of clathrin redistributed, conforming to the new cellular shape. Cytoplasmic areas, largely devoid of fluorescent dots, were observed at the cell''s periphery. In vitro, the native clathrin complex (clathrin plus clathrin-associated proteins (CAP)) bound up to 1 mol of actin, but when the clathrin polypeptide was separated from accompanying proteins it bound up to 2 mol of actin from solution. Clathrin molecular lattices may have an affinity for arrays of actin microfilaments, following them closely. Clathrin lattices display lateral mobility during cytoplasmic reorganization.