Localization of clathrin light-chain sequences mediating heavy-chain binding and coated vesicle diversity.
At least four distinct forms of clathrin light chains are found in mammalian cells. This molecular variability derives from tissue-specific patterns of expression of LCa and LCb genes. Sequence analysis shows an overall homology of 60% between LCa and LCb and the presence of brain-specific insertion sequences. These findings suggest that the different light chains have both shared and specialized functions. To address this question we have used a panel of monoclonal antibodies to identify two structurally and functionally distinct regions in the clathrin light-chain sequences. One region (residues 158-208) is exposed in native clathrin structures (triskelions and coated vesicles) and includes the brain-specific insertion sequences. The second region (residues 93-157), which is cryptic in native clathrin structures, is involved in binding the clathrin heavy chain and contains the region of strongest homology with intermediate filament proteins.
D000311:Adrenal Glands / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001921:Brain / Q000502:physiology; D002417:Cattle; D002966:Clathrin / Q000276:immunology / Q000378:metabolism*; D003034:Coated Pits, Cell-Membrane / Q000648:ultrastructure*; D011992:Endosomes / Q000648:ultrastructure*; D000939:Epitopes; D009024:Morphogenesis; D010446:Peptide Fragments / Q000276:immunology; D011485:Protein Binding; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D002966:Clathrin; D000939:Epitopes; D010446:Peptide Fragments