Reference: Terrell J, et al. (1998) A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol Cell 1(2):193-202

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Abstract


Modification of an S. cerevisiae G protein-coupled receptor with ubiquitin is required for its ligand-stimulated internalization. We now demonstrate that monoubiquitination on a single lysine residue is sufficient to signal receptor internalization, a modification distinct from that required for proteasome recognition. Formation of a polyubiquitin chain is not necessary, as demonstrated by the ability of mutant ubiquitins that lack lysine residues to serve as efficient internalization signals. Fusion of ubiquitin in-frame to a receptor that lacks cytoplasmic tail lysines also promotes rapid receptor internalization, indicating that ubiquitin itself and not a specific type of linkage to the receptor acts as an internalization signal. Thus, we have defined a cellular function for monoubiquitination in alpha-factor receptor endocytosis.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Terrell J, Shih S, Dunn R, Hicke L
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