InterPro domain: IPR037256

Association with the SNF1 complex (ASC) domain is found in the Sip1/Sip2/Gal83/AMPKbeta subunits of the SNF1/AMP-activated protein kinase (AMPK) complex [ 1 ]. SNF1/AMPK are heterotrimeric enzymes composed of a catalytic alpha-subunit, a regulatory gamma-subunit and a regulatory/targeting beta-subunit [ 2 ]. Saccharomyces cerevisiae encodes three beta-subunit genes, Sip1, Sip2 and Gal83 [ 3 , 4 ]. The beta-subunits function as target selective adaptors that recruit the catalytic kinase and regulator Snf4/gamma-subunits. The ASC domain is required for interaction with Snf4 [ 5 , 5 ].

The SNF1 kinase complex is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation [ 5 , 6 ]. As glucose levels decrease, Snf1 is activated and promotes the use of alternative carbon sources.

Structurally, this domain comprises three short helices and 3-stranded meander beta-sheet which makes extensive intermolecular interactions.

1. Domain fusion between SNF1-related kinase subunits during plant evolution. EMBO Rep. 2, 55-60
2. The Snf1 protein kinase and its activating subunit, Snf4, interact with distinct domains of the Sip1/Sip2/Gal83 component in the kinase complex. Mol. Cell. Biol. 17, 2099-106
3. A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex. EMBO J. 13, 5878-86
4. beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J. 19, 4936-43
5. SNF1/AMPK pathways in yeast. Front. Biosci. 13, 2408-20
6. Roles of the AMP-activated/SNF1 protein kinase family in the response to cellular stress. Biochem. Soc. Symp. 64, 13-27