期刊
BIOCHEMICAL JOURNAL
卷 478, 期 2, 页码 357-375出版社
PORTLAND PRESS LTD
DOI: 10.1042/BCJ20200722
关键词
-
资金
- CSC (China)
- Concerted Research Action grant [GOA/13/006]
- Interuniversity Attraction Poles grant (I.A.P. Network) [P7/40]
Multiple starvation-induced, high-affinity nutrient transporters in yeast act as receptors for activation of the PKA pathway upon re-addition of their substrates. These transceptors physically interact with the PKA-related Sch9 protein kinase, suggesting a nutrient transceptor-Sch9-TOR axis that may be affected by environmental challenges.
Multiple starvation-induced, high-affinity nutrient transporters in yeast function as receptors for activation of the protein kinase A (PKA) pathway upon re-addition of their substrate. We now show that these transceptors may play more extended roles in nutrient regulation. The Gap1 amino acid, Mep2 ammonium, Pho84 phosphate and Sull sulfate transceptors physically interact in vitro and in vivo with the PKA-related Sch9 protein kinase, the yeast homolog of mammalian S6 protein kinase and protein kinase B. Sch9 is a phosphorylation target of TOR and well known to affect nutrient-controlled cellular processes, such as growth rate. Mapping with peptide microarrays suggests specific interaction domains in Gap1 for Sch9 binding. Mutagenesis of the major domain affects the upstart of growth upon the addition of L-citrulline to nitrogen-starved cells to different extents but apparently does not affect in vitro binding. It also does not correlate with the drop in L-citrulline uptake capacity or transceptor activation of the PKA target trehalase by the Gap1 mutant forms. Our results reveal a nutrient transceptor-Sch9-TOR axis in which Sch9 accessibility for phosphorylation by TOR may be affected by nutrient transceptor-Sch9 interaction under conditions of nutrient starvation or other environmental challenges.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据