Abstract
Cell cycle arrest of Saccharomyces cerevisiae in G1 by the antimitogen alpha-factor is mediated by activation of a signal transduction pathway that results in inhibition of the cyclin-dependent kinase Cdc28-Cln. The Far1 protein is required for cell cycle arrest and associates with the Cdc28-Cln complex. The kinase activity of Cdc28-Cln was directly inhibited by Far1 both in vivo and in vitro, thus demonstrating that Far1 acts at the final step in the alpha-factor response pathway by inhibiting a G1 cyclin-dependent kinase.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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CDC28 Protein Kinase, S cerevisiae / antagonists & inhibitors*
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CDC28 Protein Kinase, S cerevisiae / metabolism
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Cell Cycle Proteins*
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Cyclin-Dependent Kinase Inhibitor Proteins
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Cyclins / genetics
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Cyclins / metabolism*
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Fungal Proteins / metabolism
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Fungal Proteins / pharmacology*
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G1 Phase
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Mating Factor
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Peptides / pharmacology
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Phosphorylation
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Protamine Kinase / metabolism
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Recombinant Fusion Proteins / metabolism
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Recombinant Fusion Proteins / pharmacology
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Repressor Proteins*
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae Proteins*
Substances
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CLN2 protein, S cerevisiae
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Cell Cycle Proteins
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Cyclin-Dependent Kinase Inhibitor Proteins
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Cyclins
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FAR1 protein, S cerevisiae
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Fungal Proteins
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Peptides
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Recombinant Fusion Proteins
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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Mating Factor
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Protamine Kinase
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CDC28 Protein Kinase, S cerevisiae