Pib2 is a cysteine sensor involved in TORC1 activation in Saccharomyces cerevisiae

Zeng, Qingzhong; Araki, Yasuhiro; Noda, Takeshi

Cell Reports, 2024, 43, 113599

Number of Access:349（2025-07-20 17:13 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/93531

Link to primary information 

File Format Terms of use Size Views Date.Available Description information
CellRep_43_113599 pdf None 5.54 MB 93 2024.02.01  
Creative Commons : Attribution

Item Information

Output File Export EndNote Basic Export Mendeley

Title
Pib2 is a cysteine sensor involved in TORC1 activation in Saccharomyces cerevisiae
Creator
CreatorName
Zeng, Qingzhong
NRID
1000060345254 1000060345254
researchmap permalink
read0080496 read0080496
Scopus Author ID
57196546306 57196546306
CreatorName
Araki, Yasuhiro
NRID
1000000290908 1000000290908
ORCID
0000-0003-3581-7961 0000-0003-3581-7961
researchmap permalink
takenoda takenoda
Scopus Author ID
7402500250 7402500250
CreatorName
Noda, Takeshi
Subject
CP: Molecular biology
Cysteine
mTORC1
Pib2
TORC1
Description
Zeng Q., Araki Y., Noda T.. Pib2 is a cysteine sensor involved in TORC1 activation in Saccharomyces cerevisiae. Cell Reports 43, 113599 (2024); https://doi.org/10.1016/j.celrep.2023.113599.
Abstract
Target of rapamycin complex 1 (TORC1) is a master regulator that monitors the availability of various amino acids to promote cell growth in Saccharomyces cerevisiae. It is activated via two distinct upstream pathways: the Gtr pathway, which corresponds to mammalian Rag, and the Pib2 pathway. This study shows that Ser3 was phosphorylated exclusively in a Pib2-dependent manner. Using Ser3 as an indicator of TORC1 activity, together with the established TORC1 substrate Sch9, we investigated which pathways were employed by individual amino acids. Different amino acids exhibited different dependencies on the Gtr and Pib2 pathways. Cysteine was most dependent on the Pib2 pathway and increased the interaction between TORC1 and Pib2 in vivo and in vitro. Moreover, cysteine directly bound to Pib2 via W632 and F635, two critical residues in the T(ail) motif that are necessary to activate TORC1. These results indicate that Pib2 functions as a sensor for cysteine in TORC1 regulation.
Publisher
Elsevier B.V.
Source Title
Cell Reports
Volume (Issue)
43
Page
113599
Date of Issued
2024-01-23
Language
English
Handle URL
https://hdl.handle.net/11094/93531
eISSN
22111247
Relation.isIdenticalTo
DOI (Publisher Version)
https://doi.org/10.1016/j.celrep.2023.113599
Access Rights
open access
CopyRight
This article is licensed under a Creative Commons Attribution 4.0 International License.
oaire:version
Version of Record
Category
学術雑誌論文 Journal Article