Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface.

The diversity of plasma membrane (PM) proteins presents a challenge for the achievement of cargo-specific regulation of endocytosis. Here, we describe a family of proteins in yeast (ARTs, for arrestin-related trafficking adaptors) that function by targeting specific PM proteins to the endocytic system. Two members (Art1 and Art2) of the ...
family were discovered in chemical-genetic screens, and they direct downregulation of distinct amino acid transporters triggered by specific stimuli. Sequence analysis revealed a total of nine ART family members in yeast. In addition to similarity to arrestins, the ARTs each contain multiple PY motifs. These motifs are required for recruitment of the Rsp5/Nedd4-like ubiquitin ligase, which modifies the cargoes as well as the ARTs. As a result, ubiquitinated cargoes are internalized and targeted to the vacuole (lysosome) for degradation. We propose that ARTs provide a cargo-specific quality-control pathway that mediates endocytic downregulation by coupling Rsp5/Nedd4 to diverse plasma membrane proteins.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Arrestin, Carrier Proteins, Cell Membrane, Endocytosis, Endosomal Sorting Complexes Required for Transport, Fungal Proteins, Lysosomes, Models, Biological, Molecular Sequence Data, Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Ubiquitin, Ubiquitin-Protein Ligase Complexes
Cell
Date: Nov. 14, 2008
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