Genetic interactions indicate a role for Mdg1p and the SH3 domain protein Bem1p in linking the G-protein mediated yeast pheromone ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-10

AUTHORS

E. Leberer, T. Leeuw, D. Harcus, D. Y. Thomas, J. Chenevert, I. Herskowitz

ABSTRACT

The pheromone signal in the yeastSaccharomyces cerevisiae is transmitted by theβ andγ subunits of the mating response G-protein. TheSTE20 gene, encoding a protein kinase required for pheromone signal transduction, has recently been identified in a genetic screen for high-gene-dosage suppressors of a partly defective Gβ mutation. The same genetic screen identifiedBEM1, which encodes an SH3 domain protein required for polarized morphogenesis in response to pheromone, and a novel gene, designatedMDG1 (multicopy suppressor ofdefectiveG-protein). TheMDG1 gene was independently isolated in a search for multicopy suppressors of abem1 mutation. TheMDG1 gene encodes a predicted hydrophilic protein of 364 amino acids with a molecular weight of 41 kDa that has no homology with known proteins. A fusion of Mdg1p with the green fluorescent protein fromAequorea victoria localizes to the plasma membrane, suggesting that Mdg1p is an extrinsically bound membrane protein. Deletion ofMDG1 causes sterility in cells in which the wild-type Gβ has been replaced by partly defective Gβ derivatives but does not cause any other obvious phenotypes. The mating defect of cells deleted forSTE20 is partially suppressed by multiple copies ofBEM1 andCDC42, which encodes a small GTP-binding protein that binds to Ste20p and is necessary for the development of cell polarity. Elevated levels ofSTE20 andBEM1 are capable of suppressing a temperature-sensitive mutation inCDC42. This complex network of genetic interactions points to a role for Bem1p and Mdg1p in G-protein mediated signal transduction and indicates a functional linkage between components of the pheromone signalling pathway and regulators of cell polarity during yeast mating. More... »

PAGES

608-621

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02172407

DOI

http://dx.doi.org/10.1007/bf02172407

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010832788

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8914522


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68 dosage suppressors
69 elevated levels
70 functional linkage
71 fusion
72 genes
73 genetic interactions
74 genetic screen
75 homology
76 hydrophilic protein
77 interaction
78 interaction point
79 kinase
80 levels
81 linkage
82 mating
83 mating defect
84 mating response G-protein
85 mediated signal transduction
86 membrane
87 membrane proteins
88 molecular weight
89 morphogenesis
90 multicopy suppressor
91 multiple copies
92 mutations
93 network
94 novel genes
95 obvious phenotype
96 pathway
97 phenotype
98 pheromone
99 pheromone signal transduction
100 pheromone signals
101 plasma membrane
102 point
103 polarity
104 polarized morphogenesis
105 protein
106 protein kinase
107 regulator
108 response
109 role
110 screen
111 search
112 signal transduction
113 signals
114 small GTP-binding proteins
115 sterility
116 subunits
117 suppressor
118 transduction
119 weight
120 yeast mating
121 yeast pheromone
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