title: Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller.
abstract: The amino-terminal domain of the clathrin heavy chain, which folds into a seven-bladed beta-propeller, binds directly to several endocytic proteins via short sequences based on the consensus residues LLDLD. In addition to a single LLDLD-based, type I clathrin-binding sequence, both amphiphysin and epsin contain a second, distinct sequence that is also capable of binding to clathrin directly. Here, we analyzed these sequences, which we term type II sequences, and show that the (257)LMDLA sequence in rat epsin 1 appears to be a weak clathrin-binding variant of the sequence (417)PWDLW originally found in human amphiphysin II. The structural features of the type II sequence required for association with clathrin are distinct from the LLDLD-based sequence. In the central segment of amphiphysin, the type I and type II sequences cooperate to effect optimal clathrin binding and the formation of sedimentable assemblies. Together, the data provide evidence for two interaction surfaces upon certain endocytic accessory proteins that could cooperate with other coat components to enhance clathrin bud formation at the cell surface.
authors.affiliation: Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
authors.forename: M T
authors.initials: MT
authors.lastname: Drake
authors.forename: L M
authors.initials: LM
authors.lastname: Traub
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002966:Clathrin / Q000737:chemistry* / Q000378:metabolism*; D003001:Cloning, Molecular; D016384:Consensus Sequence; D003600:Cytosol / Q000378:metabolism; D004705:Endocytosis; D004926:Escherichia coli; D005982:Glutathione Transferase / Q000378:metabolism; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D002966:Clathrin; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; C075637:amphiphysin; D005982:Glutathione Transferase