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Molecular basis for recognition of dilysine trafficking motifs by COPI.
|Title||Molecular basis for recognition of dilysine trafficking motifs by COPI.|
|Publication Type||Journal Article|
|Year of Publication||2012|
|Authors||Jackson LP, Lewis M, Kent HM, Edeling MA, Evans PR, Duden R, Owen DJ|
|Date Published||2012 Dec 11|
COPI mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) and within the Golgi stack, sorting transmembrane proteins bearing C-terminal KKxx or KxKxx motifs. The structure of KxKxx motifs bound to the N-terminal WD-repeat domain of β'-COP identifies electrostatic contacts between the motif and complementary patches at the center of the β'-COP propeller. An absolute requirement of a two-residue spacing between the terminal carboxylate group and first lysine residue results from interactions of carbonyl groups in the motif backbone with basic side chains of β'-COP. Similar interactions are proposed to mediate binding of KKxx motifs by the homologous α-COP domain. Mutation of key interacting residues in either domain or in their cognate motifs abolishes in vitro binding and results in mistrafficking of dilysine-containing cargo in yeast without compromising cell viability. Flexibility between β'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly.
|Alternate Journal||Dev. Cell|