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Molecular basis for recognition of dilysine trafficking motifs by COPI.


ABSTRACT: 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 ?'-COP identifies electrostatic contacts between the motif and complementary patches at the center of the ?'-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 ?'-COP. Similar interactions are proposed to mediate binding of KKxx motifs by the homologous ?-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 ?'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly.

SUBMITTER: Jackson LP 

PROVIDER: S-EPMC3521961 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Molecular basis for recognition of dilysine trafficking motifs by COPI.

Jackson Lauren P LP   Lewis Michael M   Kent Helen M HM   Edeling Melissa A MA   Evans Philip R PR   Duden Rainer R   Owen David J DJ  

Developmental cell 20121121 6


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 res  ...[more]

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