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FASEB J

Title:		Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
Author(s):		Hicke L;
Address:		"Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500, USA"
Journal Title:		FASEB J
Year:		1997
Volume:		11
Issue:		14
Page Number:		1215 - 1226
DOI:		10.1096/fasebj.11.14.9409540
ISSN/ISBN:		0892-6638 (Print) 0892-6638 (Linking)
Abstract:		"The modification of cytosolic proteins with polyubiquitin chains targets them for recognition and degradation by the multisubunit proteolytic particle, the 26S proteasome. Membrane proteins are also substrates for ubiquitination. Integral membrane proteins of the endoplasmic reticulum are ubiquitinated and destroyed by the proteasome. However, it has been shown recently that the ubiquitination of Saccharomyces cerevisiae plasma membrane proteins signals their degradation by the proteolytic system in the lysosome-like vacuole. Ubiquitination of several different classes of cell surface proteins serves as a signal for their entry into the endocytic pathway; this leads to their transport to the vacuole, where they are permanently inactivated by degradation. In yeast, ubiquitin has been implicated as an internalization signal for most, if not all, endogenous plasma membrane proteins that are known to be endocytosed. Ubiquitin-dependent internalization has been best characterized for two proteins: the mating pheromone alpha-factor receptor and the uracil permease. Some mammalian cell surface receptors are also ubiquitinated at the plasma membrane. Ubiquitination machinery is required for ligand-induced endocytosis of the growth hormone receptor, suggesting that ubiquitin-dependent endocytosis and sorting is also an important regulatory process in mammalian cells. Mammalian receptors may also be down-regulated through the degradation of their cytosolic domains by a proteasome-dependent pathway"
Keywords:		"Animals Cell Membrane/*metabolism Fungal Proteins/metabolism Humans In Vitro Techniques Mammals Membrane Proteins/*metabolism Membrane Transport Proteins/metabolism *Nucleotide Transport Proteins Phosphorylation Receptors, Growth Factor/metabolism Recepto;"
Notes:		"MedlineHicke, L eng Review 1997/12/31 FASEB J. 1997 Dec; 11(14):1215-26. doi: 10.1096/fasebj.11.14.9409540"