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Phosphorylation of Golgin Imh1 by AMPK/Snf1 compromises Golgi compartmentalization by releasing Arl1-Imh1 axis.

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Τίτλος: Phosphorylation of Golgin Imh1 by AMPK/Snf1 compromises Golgi compartmentalization by releasing Arl1-Imh1 axis.
Συγγραφείς: Cai PJ; Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100225, Taiwan., Yu CJ; Department of Cell and Molecular Biology, College of Medicine, Chang Gung University, Taoyuan 333323, Taiwan.; Department of Thoracic Medicine, Chang Gung Memorial Hospital, Taoyuan 333423, Taiwan., Lee FS; Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100225, Taiwan.; Department of Medical Research, National Taiwan University Hospital, Taipei 100225, Taiwan.
Πηγή: Molecular biology of the cell [Mol Biol Cell] 2025 Aug 01; Vol. 36 (8), pp. ar96. Date of Electronic Publication: 2025 Jun 25.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: American Society for Cell Biology Country of Publication: United States NLM ID: 9201390 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1939-4586 (Electronic) Linking ISSN: 10591524 NLM ISO Abbreviation: Mol Biol Cell Subsets: MEDLINE
Imprint Name(s): Original Publication: Bethesda, MD : American Society for Cell Biology, c1992-
Ιατρικοί όροι (MeSH): Golgi Apparatus*/metabolism , Saccharomyces cerevisiae Proteins*/metabolism , Saccharomyces cerevisiae Proteins*/genetics , ADP-Ribosylation Factors*/metabolism , Protein Serine-Threonine Kinases*/metabolism , AMP-Activated Protein Kinases*/metabolism, Saccharomyces cerevisiae/metabolism ; Glucose/metabolism ; Vesicular Transport Proteins/metabolism ; Golgi Matrix Proteins/metabolism ; Phosphorylation ; Protein Transport ; Monomeric GTP-Binding Proteins
Περίληψη: 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 Imh1S606D,S802D,S804D mislocalizes away from the Golgi, while the phospho-deficient mutant Imh1S606A,S802A,S804A, prevents this mislocalization in an Arl1-dependent manner under glucose deprivation, indicating that this change is not due to Arl1 inactivation. We also provide evidence that AMPK/Snf1 associates with Imh1 and directly phosphorylates Imh1, resulting in conformational change. Furthermore, we demonstrate that AMPK/Snf1-regulated Imh1 phosphorylation impairs its ability to support SNARE recycling in ypt6Δ mutants and compromises Golgi homeostasis. Collectively, these findings reveal how AMPK/Snf1-mediated phosphorylation drives the disassembly of the Arl1-Imh1 axis from the Golgi in response to low-energy conditions, highlighting the critical role of Imh1 phosphorylation in regulating Golgi function.
Competing Interests: Conflict of interest: The authors declare no financial conflict of interest.
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Substance Nomenclature: 0 (Saccharomyces cerevisiae Proteins)
EC 3.6.1.- (ARL1 protein, S cerevisiae)
EC 3.6.5.2 (ADP-Ribosylation Factors)
EC 2.7.11.1 (Protein Serine-Threonine Kinases)
EC 2.7.1.- (SNF1-related protein kinases)
IY9XDZ35W2 (Glucose)
EC 2.7.11.31 (AMP-Activated Protein Kinases)
0 (Vesicular Transport Proteins)
0 (Golgi Matrix Proteins)
EC 3.6.5.2 (Monomeric GTP-Binding Proteins)
Entry Date(s): Date Created: 20250625 Date Completed: 20250717 Latest Revision: 20260813
Update Code: 20260813
PubMed Central ID: PMC12367314
DOI: 10.1091/mbc.E25-02-0084
PMID: 40560401
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:1939-4586
DOI:10.1091/mbc.E25-02-0084