Nutrient transceptors physically interact with the yeast S6/protein kinase B homolog, Sch9, a TOR kinase target

Zhang, Zhiqiang; Cottignie, Ines; Zeebroeck, Griet Van; Thevelein, Johan M.

doi:10.1042/bcj20200722

Cited by 8 publications

(3 citation statements)

References 85 publications

(75 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…If differences in substrate motifs of PKA and Sch9 do not explain why some targets are exclusively phosphorylated by PKA, different localization of the kinases relative to their targets may be invoked. Sch9 is present both in association with the vacuolar membrane and dispersed throughout the cytoplasm [ 26 , 169 , 170 ] and a recent study detected pools of Sch9 at additional locations, including the plasma membrane and nucleo-vacuolar junction [ 171 ]. As discussed below, our understanding of the subcellular localizations of PKA is still far from complete, but it is at least partially found in the cytoplasm.…”

Section: Substrate Specificity Of Pka and Sch9mentioning

confidence: 99%

Interaction of TOR and PKA Signaling in S. cerevisiae

Plank

2022

Biomolecules

View full text Add to dashboard Cite

TOR and PKA signaling are the major growth-regulatory nutrient-sensing pathways in S. cerevisiae. A number of experimental findings demonstrated a close relationship between these pathways: Both are responsive to glucose availability. Both regulate ribosome production on the transcriptional level and repress autophagy and the cellular stress response. Sch9, a major downstream effector of TORC1 presumably shares its kinase consensus motif with PKA, and genetic rescue and synthetic defects between PKA and Sch9 have been known for a long time. Further, studies in the first decade of this century have suggested direct regulation of PKA by TORC1. Nonetheless, the contribution of a potential direct cross-talk vs. potential sharing of targets between the pathways has still not been completely resolved. What is more, other findings have in contrast highlighted an antagonistic relationship between the two pathways. In this review, I explore the association between TOR and PKA signaling, mainly by focusing on proteins that are commonly referred to as shared TOR and PKA targets. Most of these proteins are transcription factors which to a large part explain the major transcriptional responses elicited by TOR and PKA upon nutrient shifts. I examine the evidence that these proteins are indeed direct targets of both pathways and which aspects of their regulation are targeted by TOR and PKA. I further explore if they are phosphorylated on shared sites by PKA and Sch9 or when experimental findings point towards regulation via the PP2ASit4/PP2A branch downstream of TORC1. Finally, I critically review data suggesting direct cross-talk between the pathways and its potential mechanism.

show abstract

Section: Substrate Specificity Of Pka and Sch9mentioning

confidence: 99%

Interaction of TOR and PKA Signaling in S. cerevisiae

Plank

2022

Biomolecules

View full text Add to dashboard Cite

show abstract

“…One of the unique features of transceptors is that they activate the PKA signaling cascade without an increase in the cAMP level. Some transceptors, such as Gap1, Mep2, Sul1, and Pho84, directly interact with the protein kinase Sch9, which is a phosphorylated substrate of TORC1 and affects nutrient‐controlled cellular processes (Zhang et al, 2021). These data imply that the interaction or dissociation status of transceptors with intracellular proteins may regulate cellular processes.…”

Section: Discussionmentioning

confidence: 99%

The arginine transporter Can1 acts as a transceptor for regulation of proline utilization in the yeast Saccharomyces cerevisiae

Tanahashi

Nishimura

Morita

et al. 2023

Yeast

View full text Add to dashboard Cite

Proline is the most abundant amino acid in wine and beer, because the yeast Saccharomyces cerevisiae hardly assimilates proline during fermentation processes. Our previous studies showed that arginine induces endocytosis of the proline transporter Put4, resulting in inhibition of proline utilization. We here report a possible role of arginine sensing in the inhibition of proline utilization. We first found that two basic amino acids, ornithine, and lysine, inhibit proline utilization by inducing Put4 endocytosis in a manner similar to arginine, but citrulline does not. Our genetic screening revealed that the arginine transporter Can1 is involved in the inhibition of proline utilization by arginine. Intriguingly, the arginine uptake activity of Can1 was not required for the arginine‐dependent inhibition of proline utilization, suggesting that Can1 has a function beyond its commonly known function of transporting arginine. More importantly, our biochemical analyses revealed that Can1 activates signaling cascades of protein kinase A in response to extracellular arginine. Hence, we proposed that Can1 regulates proline utilization by functioning as a transceptor possessing the activity of both a transporter and receptor of arginine.

show abstract

“…Nutrient repletion releases the Tpks to activate proliferation-specific targets. Sch9 also binds to high-affinity transporters, suggesting a similar mechanism of regulation (210).…”

Section: Signaling Pathways For Quiescence Entrymentioning

confidence: 99%

Quiescence in Saccharomyces cerevisiae

Breeden

Tsukiyama

2022

Annu. Rev. Genet.

View full text Add to dashboard Cite

Most cells live in environments that are permissive for proliferation only a small fraction of the time. Entering quiescence enables cells to survive long periods of nondivision and reenter the cell cycle when signaled to do so. Here, we describe what is known about the molecular basis for quiescence in Saccharomyces cerevisiae, with emphasis on the progress made in the last decade. Quiescence is triggered by depletion of an essential nutrient. It begins well before nutrient exhaustion, and there is extensive crosstalk between signaling pathways to ensure that all proliferation-specific activities are stopped when any one essential nutrient is limiting. Every aspect of gene expression is modified to redirect and conserve resources. Chromatin structure and composition change on a global scale, from histone modifications to three-dimensional chromatin structure. Thousands of proteins and RNAs aggregate, forming unique structures with unique fates, and the cytoplasm transitions to a glass-like state.

show abstract

Nutrient transceptors physically interact with the yeast S6/protein kinase B homolog, Sch9, a TOR kinase target

Cited by 8 publications

References 85 publications

Interaction of TOR and PKA Signaling in S. cerevisiae

Interaction of TOR and PKA Signaling in S. cerevisiae

The arginine transporter Can1 acts as a transceptor for regulation of proline utilization in the yeast Saccharomyces cerevisiae

Quiescence in Saccharomyces cerevisiae

Contact Info

Product

Resources

About