Title: Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-pheromone receptor in yeast
Authors : Rohrer, Jack
Bénédetti, Hélène
Zanolari, Bettina
Riezman, Howard
Published in : Molecular Biology of the Cell
Volume(Issue) : 4
Issue : 5
Pages : 511
Pages to: 521
Publisher / Ed. Institution : American Society for Cell Biology
Issue Date: May-1993
License (according to publishing contract) : Licence according to publishing contract
Type of review: Peer review (Publication)
Language : English
Subject (DDC) : 571: Physiology and related subjects
572: Biochemistry
Abstract: The Saccharomyces cerevisiae alpha-pheromone receptor, a polytopic, G protein-coupled, membrane protein, is internalized after binding of alpha-factor. Mutational analysis suggested that the first 39 residues of the receptor's cytoplasmic tail carries sufficient information for internalization. A point mutation in one of these 39 residues, K337 to R337, renders the receptor nonfunctional for endocytosis. Other residues, D335 and S338, contribute to the efficiency of internalization. When the sequence DAKSS is added onto a severely truncated receptor, endocytosis of the receptor is restored, showing that this sequence functions to mediate or to signal interaction with the endocytic machinery. Analysis of pheromone response and recovery in strains expressing mutant receptors suggests that receptor internalization is not important for response but contributes to recovery from pheromone.
Departement: Life Sciences und Facility Management
Publication type: Article in scientific Journal
DOI : 10.1091/mbc.4.5.511
ISSN: 1939-4586
URI: https://digitalcollection.zhaw.ch/handle/11475/6798
Appears in Collections:Publikationen Life Sciences und Facility Management

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