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.
Predicate | Object |
---|---|
rdf:type | |
rdfs:comment |
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.
|
skos:exactMatch | |
uniprot:name |
Science
|
uniprot:author |
Herskowitz I.,
Peter M.
|
uniprot:date |
1994
|
uniprot:pages |
1228-1231
|
uniprot:title |
Direct inhibition of the yeast cyclin-dependent kinase Cdc28-Cln by Far1.
|
uniprot:volume |
265
|
dc-term:identifier |
doi:10.1126/science.8066461
|