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Site‐specific disruption of clathrin assembly produces novel structures.
Author(s) -
Blank G.S.,
Brodsky F.M.
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04470.x
Subject(s) - clathrin , endocytosis , biology , vesicle , biophysics , microbiology and biotechnology , biochemistry , receptor , membrane
Clathrin assembly in vitro produces a highly ordered polyhedral structure (basket). This resembles clathrin assembled in situ on coated pits and vesicles which form during receptor‐mediated endocytosis. Sites on clathrin involved in assembly were identified by assembling clathrin in the presence of anti‐clathrin monoclonal antibodies. Three of the antibodies, as IgG, prevented the assembly of normal baskets, and their Fab fragments induced formation of two types of novel clathrin structures. Antibody effects on assembly and competitive binding data indicate these antibodies bind to two sites, critical for clathrin interactions, located in the same region of the clathrin heavy chain. Analysis of novel structures formed, suggested that nucleation but not further assembly was occurring, implying an ordered sequence of clathrin interactions during assembly.