A family of proteins containing a conserved domain that mediates interaction with the XXXX SNF1 protein kinase complex.

@entity375 @entity69989 @entity535 @entity69990 @entity563 @entity69991 @entity1889 @entity413
The SNF1 protein kinase is required for the regulatory response to @entity413 starvation in @entity375 . SNF1 is a protein @entity563 / @entity1889 kinase that has been widely conserved in both plants and mammals. Previously, we identified @entity69990 and @entity69991 as proteins that interact with SNF1 in vivo by the two-hybrid system. We have cloned the @entity69991 gene and the encoded protein is homologous to @entity69990 and to @entity69989 , which affects @entity413 repression of the GAL genes. We show that @entity69991 and @entity69989 , like @entity69990 , co-immunoprecipitate with SNF1 and are phosphorylated in vitro. An 80 @entity535 sequence, designated the ASC domain, is highly conserved at the C-termini of all three proteins. We show that this small domain can mediate protein-protein interaction with the SNF1 kinase complex. Thus, @entity69990 , @entity69991 and @entity69989 define a family of homologous proteins that are tightly associated with the SNF1 kinase, probably in alternative forms of the complex. Genetic evidence suggests that the three proteins have distinct, but related, functions in the SNF1 pathway, and deletion of @entity69989 dramatically reduces SNF1 activity in immune complex assays. We propose that @entity69990 , @entity69991 and @entity69989 act as adaptors that promote the activity of SNF1 towards specific targets.
