ArticleThe Journal of biological chemistry2011
Yeast 3-phosphoinositide-dependent protein kinase-1 (PDK1) orthologs Pkh1-3 differentially regulate phosphorylation of protein kinase A (PKA) and the protein kinase B (PKB)/S6K ortholog Sch9.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 59 citations in OpenAlex.
- Regulatory dynamics of Sch9 in response to cytosolic acidification: From spatial reconfiguration to cellular adaptation to stresses.iScience · 2025Article
- The Yeast Protein Kinase Sch9 Functions as a Central Nutrient-Responsive Hub That Calibrates Metabolic and Stress-Related Responses.Journal of fungi (Basel, Switzerland) · 2023Review
- The nutrient-responsive CDK Pho85 primes the Sch9 kinase for its activation by TORC1.PLoS genetics · 2023Article
- Exploring the anti-aging potential of natural products and plant extracts in budding yeastF1000Research · 2023Review
- HSF1 induces RNA polymerase II synthesis of ribosomal RNA in S. cerevisiae during nitrogen deprivation.Current genetics · 2021Article
- The 3-phosphoinositide-dependent protein kinase 1 is an essential upstream activator of protein kinase A in malaria parasites.PLoS biology · 2021Article
- Nutrient transceptors physically interact with the yeast S6/protein kinase B homolog, Sch9, a TOR kinase target.The Biochemical journal · 2021Article
- PDK1 regulates auxin transport and Arabidopsis vascular development through AGC1 kinase PAX.Nature plants · 2020Article
- Pkh1p-Ypk1p and Pkh1p-Sch9p Pathways Are Activated by Acetic Acid to Induce a Mitochondrial-Dependent Regulated Cell Death.Oxidative medicine and cellular longevity · 2020Article
- pH homeostasis links the nutrient sensing PKA/TORC1/Sch9 ménage-à-trois to stress tolerance and longevity.Microbial cell (Graz, Austria) · 2018Review
- Multiple Transceptors for Macro- and Micro-Nutrients Control Diverse Cellular Properties Through the PKA Pathway in Yeast: A Paradigm for the Rapidly Expanding World of Eukaryotic Nutrient Transceptors Up to Those in Human Cells.Frontiers in pharmacology · 2018Review
- The ceramide activated protein phosphatase Sit4 impairs sphingolipid dynamics, mitochondrial function and lifespan in a yeast model of Niemann-Pick type C1.Biochimica et biophysica acta. Molecular basis of disease · 2018Article
- COCurrent genetics · 2017Review
- The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.Biomolecules · 2017Review
- The yeast protein kinase Sch9 adjusts V-ATPase assembly/disassembly to control pH homeostasis and longevity in response to glucose availability.PLoS genetics · 2017Article
- Nutrient Sensing at the Plasma Membrane of Fungal Cells.Microbiology spectrum · 2017Review
- Article
- The Aspergillus fumigatus SchAMolecular microbiology · 2016Article
- Prostaglandin E2 stimulates normal bronchial epithelial cell growth through induction of c-Jun and PDK1, a kinase implicated in oncogenesis.Respiratory research · 2015Article
- Depletion of yeast PDK1 orthologs triggers a stress-like transcriptional response.BMC genomics · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pkh1, -2, and -3 are the yeast orthologs of mammalian 3-phosphoinositide-dependent protein kinase-1 (PDK1). Although essential for viability, their functioning remains poorly understood. Sch9, the yeast protein kinase B and/or S6K ortholog, has been identified as one of their targets. We now have shown that in vitro interaction of Pkh1 and Sch9 depends on the hydrophobic PDK1-interacting fragment pocket in Pkh1 and requires the complementary hydrophobic motif in Sch9. We demonstrated that Pkh1 phosphorylates Sch9 both in vitro and in vivo on its PDK1 site and that this phosphorylation is essential for a wild type cell size. In vivo phosphorylation on this site disappeared during nitrogen deprivation and rapidly increased again upon nitrogen resupplementation. In addition, we have shown here for the first time that the PDK1 site in protein kinase A is phosphorylated by Pkh1 in vitro, that this phosphorylation is Pkh-dependent in vivo and occurs during or shortly after synthesis of the protein kinase A catalytic subunits. Mutagenesis of the PDK1 site in Tpk1 abolished binding of the regulatory subunit and cAMP dependence. As opposed to PDK1 site phosphorylation of Sch9, phosphorylation of the PDK1 site in Tpk1 was not regulated by nitrogen availability. These results bring new insight into the control and prevalence of PDK1 site phosphorylation in yeast by Pkh protein kinases.
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