ArticleMolecular and cellular biology1997
The Snf1 protein kinase and its activating subunit, Snf4, interact with distinct domains of the Sip1/Sip2/Gal83 component in the kinase complex.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed, 254 citations in OpenAlex.
- AMPK alters proteasome phosphorylation status and prevents persistent proteasome condensates.Genetics · 2025Article
- Exploring carbon source related localization and phosphorylation in the Snf1/Mig1 network using population and single cell-based approaches.Microbial cell (Graz, Austria) · 2024Article
- Advances inJournal of fungi (Basel, Switzerland) · 2023Review
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- The polyHIS Tract of Yeast AMPK Coordinates Carbon Metabolism with Iron Availability.International journal of molecular sciences · 2023Article
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- Intrinsically disordered signaling proteins: Essential hub players in the control of stress responses in Saccharomyces cerevisiae.PloS one · 2022Article
- A Suppressor Mutation in the β-Subunit Kis1 Restores Functionality of the SNF1 Complex inmSphere · 2021Article
- Reg1 and Snf1 regulate stress-induced relocalization of protein phosphatase-1 to cytoplasmic granules.The FEBS journal · 2021Article
- Genome-Wide Analysis of Nutrient Signaling Pathways Conserved in Arbuscular Mycorrhizal Fungi.Microorganisms · 2021Article
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- Genome-wide identification and characterization of the AMPK genes and their distinct expression patterns in response to air exposure in the Manila clam (Ruditapes philippinarum).Genes & genomics · 2020Article
- An Intragenic Recombination Event Generates a Snf4-Independent Form of the Essential Protein Kinase Snf1 in Candida albicans.mSphere · 2019Article
- TAK1 mediates convergence of cellular signals for death and survival.Apoptosis : an international journal on programmed cell death · 2019Review
- Reciprocal Regulation of AMPK/SNF1 and Protein Acetylation.International journal of molecular sciences · 2018Review
- Conventional and emerging roles of the energy sensor Snf1/AMPK inMicrobial cell (Graz, Austria) · 2018Review
- A Bimolecular Fluorescence Complementation Tool for Identification of Protein-Protein Interactions inG3 (Bethesda, Md.) · 2017Article
- FvSNF1, the sucrose non-fermenting protein kinase gene of Fusarium virguliforme, is required for cell-wall-degrading enzymes expression and sudden death syndrome development in soybean.Current genetics · 2017Article
- Single-cell study links metabolism with nutrient signaling and reveals sources of variability.BMC systems biology · 2017Article
45 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Snf1 protein kinase plays a central role in the response to glucose starvation in the yeast Saccharomyces cerevisiae. Previously, we showed that two-hybrid interaction between Snf1 and its activating subunit, Snf4, is inhibited by high levels of glucose. These findings, together with biochemical evidence that Snf1 and Snf4 remain associated in cells grown in glucose, suggested that another protein (or proteins) anchors Snf1 and Snf4 into a complex. Here, we examine the possibility that a family of proteins, comprising Sip1, Sip2, and Gal83, serves this purpose. We first show that the fraction of cellular Snf4 protein that is complexed with Snf1 is reduced in a sip1delta sip2delta gal83delta triple mutant. We then present evidence that Sip1, Sip2, and Gal83 each interact independently with both Snf1 and Snf4 via distinct domains. A conserved internal region binds to the Snf1 regulatory domain, and the conserved C-terminal ASC domain binds to Snf4. Interactions were mapped by using the two-hybrid system and were confirmed by in vitro binding studies. These findings indicate that the Sip1/Sip2/Gal83 family anchors Snf1 and Snf4 into a complex. Finally, the interaction of the yeast Sip2 protein with a plant Snf1 homolog suggests that this function is conserved in plants.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.