ArticleMolecular biology of the cell2025
Phosphorylation of Golgin Imh1 by AMPK/Snf1 compromises Golgi compartmentalization by releasing Arl1-Imh1 axis.
Article in Molecular biology of the cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Golgins, coiled-coil proteins, are crucial for Golgi architecture and intracellular transport. Mammals have four GRIP-domain-containing Golgins, while budding yeast has a single conserved Golgin, Imh1. Imh1 is recruited to the Golgi membrane by the active small GTPase Arl1 via its GRIP domain. Despite extensive phosphorylation of Imh1 under various stress conditions observed in previous screenings, the biological significance and regulatory mechanisms of Imh1 phosphorylation remain unclear. This study reveals that Snf1, a yeast AMPK homologue, regulates the dissociation of the Arl1-Imh1 axis from the Golgi during glucose deprivation by phosphorylating Imh1 at Ser606, Ser802, and Ser804. The phosphomimetic mutant Imh1
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