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Article

Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism.

Molecular and cellular biology - 1 Jan 2004

Wiatrowski Heather A, Van Denderen Bryce J W, Berkey Cristin D, Kemp Bruce E, Stapleton David, Carlson Marian

Abstract excerpt

The yeast Snf1 kinase and its mammalian ortholog, AMP-activated protein kinase (AMPK), regulate responses to metabolic stress. Previous studies identified a glycogen-binding domain in the AMPK beta1 subunit, and the sequence is conserved in the Snf1 kinase beta subunits Gal83 and Sip2. Here we use genetic analysis to assess the role of this domain in vivo. Alteration of Gal83 at residues that are important for...

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Identifiers

PMID: 14673168
DOI: 10.1128/MCB.24.1.352-361.2004
PMCID: PMC303368

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism.PMID 14673168Read ↗

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