ArticleEukaryotic cell2006
Regulatory domains of Snf1-activating kinases determine pathway specificity.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Septin Assembly and Remodeling at the Cell Division Site During the Cell Cycle.Frontiers in cell and developmental biology · 2021Review
- The AMPK family member Snf1 protects Saccharomyces cerevisiae cells upon glutathione oxidation.PloS one · 2013Article
- Heterotrimer-independent regulation of activation-loop phosphorylation of Snf1 protein kinase involves two protein phosphatases.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Protein kinase A contributes to the negative control of Snf1 protein kinase in Saccharomyces cerevisiae.Eukaryotic cell · 2012Article
- Interaction of SNF1 protein kinase with its activating kinase Sak1.Eukaryotic cell · 2011Article
- Monitoring spindle orientation: Spindle position checkpoint in charge.Cell division · 2010Article
- The spindle position checkpoint is coordinated by the Elm1 kinase.The Journal of cell biology · 2010Article
- The checkpoint kinase Hsl1p is activated by Elm1p-dependent phosphorylation.Molecular biology of the cell · 2008Article
- Multiway real-time PCR gene expression profiling in yeast Saccharomyces cerevisiae reveals altered transcriptional response of ADH-genes to glucose stimuli.BMC genomics · 2008Article
- SNF1/AMPK pathways in yeast.Frontiers in bioscience : a journal and virtual library · 2008Review
- Mechanisms regulating the protein kinases of Saccharomyces cerevisiae.Eukaryotic cell · 2007Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
In Saccharomyces cerevisiae, the Snf1 kinase can be activated by any one of three upstream kinases, Sak1, Tos3, or Elm1. All three Snf1-activating kinases contain serine/threonine kinase domains near their N termini and large C-terminal domains with little sequence conservation and previously unknown function. Deletion of the C-terminal domains of Sak1 and Tos3 greatly reduces their ability to activate the Snf1 pathway. In contrast, deletion of the Elm1 C-terminal domain has no effect on Snf1 signaling but abrogates the ability of Elm1 to participate in the morphogenetic-checkpoint signaling pathway. Thus, the C-terminal domains of Sak1, Tos3, and Elm1 help to determine pathway specificity. Additional deletion mutants of the Sak1 kinase revealed that the N terminus of the protein is essential for Snf1 signaling. The deletion of 43 amino acids from within the N terminus of Sak1 (residues 87 to 129) completely blocks Snf1 signaling and activation loop phosphorylation in vivo. The Sak1 kinase domain (lacking both N-terminal and C-terminal domains) is catalytically active and specific in vitro but is unable to promote Snf1 signaling in vivo when expressed at normal levels. Our studies indicate that the kinase domains of the Snf1-activating kinases are not sufficient by themselves for their proper function and that the nonconserved N-terminal and C-terminal domains are critical for the biological activities of these kinases.
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