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Role of Ubiquitination in Endocytic Trafficking of G‐Protein‐Coupled Receptors
Author(s) -
Hislop James N.,
von Zastrow Mark
Publication year - 2011
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2010.01121.x
Subject(s) - endocytic cycle , ubiquitin , biology , microbiology and biotechnology , g protein coupled receptor , f box protein , downregulation and upregulation , transport protein , receptor , ubiquitin ligase , signal transduction , endocytosis , biochemistry , gene
Lysyl ubiquitination has long been known to target cytoplasmic proteins for proteasomal degradation, and there is now extensive evidence that ubiquitination functions in vacuolar/lysosomal targeting of membrane proteins from both the biosynthetic and endocytic pathways. G‐protein‐coupled receptors (GPCRs) represent the largest and most diverse family of membrane proteins, whose function is of fundamental importance both physiologically and therapeutically. In this review, we discuss the role of ubiquitination in the vacuolar/lysosomal downregulation of GPCRs through the endocytic pathway, with a primary focus on lysosomal trafficking in mammalian cells. We will summarize evidence indicating that mammalian GPCRs are regulated by ubiquitin‐dependent mechanisms conserved in budding yeast, and then consider evidence for additional ubiquitin‐dependent and ‐independent regulation that may be specific to animal cells.