Amino Acid-Sensing mTOR Signaling

2005 ◽  
Author(s):  
Jae Eun Kim ◽  
Jie Chen ◽  
Ebru Erbay
Keyword(s):  
Amino Acid ◽  
Mtor Signaling ◽  
Amino Acid Sensing

Implications of amino acid sensing and dietary protein to the aging process

2019 ◽  
Vol 115 ◽  
pp. 69-78 ◽  
Author(s):  
Oleh Lushchak ◽  
Olha M. Strilbytska ◽  
Ihor Yurkevych ◽  
Alexander M. Vaiserman ◽  
Kenneth B. Storey
Keyword(s):  
Amino Acid ◽  
Dietary Protein ◽  
Aging Process ◽  
Amino Acid Sensing

scholarly journals Activation of the SPS Amino Acid-Sensing Pathway in Saccharomyces cerevisiae Correlates with the Phosphorylation State of a Sensor Component, Ptr3

2007 ◽  
Vol 28 (2) ◽  
pp. 551-563 ◽  
Author(s):  
Zhengchang Liu ◽  
Janet Thornton ◽  
Mário Spírek ◽  
Ronald A. Butow
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Amino Acid ◽  
Nuclear Translocation ◽  
Proteolytic Processing ◽  
Casein Kinase I ◽  
Positive Regulators ◽  
Amino Acid Permeases ◽  
Amino Acid Sensing ◽  
Amino Acid Sensor

ABSTRACT Cells of the budding yeast Saccharomyces cerevisiae sense extracellular amino acids and activate expression of amino acid permeases through the SPS-sensing pathway, which consists of Ssy1, an amino acid sensor on the plasma membrane, and two downstream factors, Ptr3 and Ssy5. Upon activation of SPS signaling, two transcription factors, Stp1 and Stp2, undergo Ssy5-dependent proteolytic processing that enables their nuclear translocation. Here we show that Ptr3 is a phosphoprotein whose hyperphosphorylation is increased by external amino acids and is dependent on Ssy1 but not on Ssy5. A deletion mutation in GRR1, encoding a component of the SCFGrr1 E3 ubiquitin ligase, blocks amino acid-induced hyperphosphorylation of Ptr3. We found that two casein kinase I (CKI) proteins, Yck1 and Yck2, previously identified as positive regulators of SPS signaling, are required for hyperphosphorylation of Ptr3. Loss- and gain-of-function mutations in PTR3 result in decreased and increased Ptr3 hyperphosporylation, respectively. We found that a defect in PP2A phosphatase activity leads to the hyperphosphorylation of Ptr3 and constitutive activation of SPS signaling. Two-hybrid analysis revealed interactions between the N-terminal signal transduction domain of Ssy1 with Ptr3 and Yck1. Our findings reveal that CKI and PP2A phosphatase play antagonistic roles in SPS sensing by regulating Ptr3 phosphorylation.

S1609 Amino Acid Sensing Mechanisms in Enteroendocrine STC-1 Cells

2009 ◽  
Vol 136 (5) ◽  
pp. A-234
Author(s):  
Steven H. Young ◽  
Osvaldo Rey ◽  
Enrique Rozengurt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sensing

scholarly journals Hierarchical mechanism of amino acid sensing by the T-box riboswitch

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Krishna C. Suddala ◽  
Javier Cabello-Villegas ◽  
Malgorzata Michnicka ◽  
Collin Marshall ◽  
Edward P. Nikonowicz ◽  
...  
Keyword(s):  
Amino Acid ◽  
T Box ◽  
Amino Acid Sensing

scholarly journals Recent Advances in Understanding Amino Acid Sensing Mechanisms that Regulate mTORC1

2016 ◽  
Vol 17 (10) ◽  
pp. 1636 ◽  
Author(s):  
Liufeng Zheng ◽  
Wei Zhang ◽  
Yuanfei Zhou ◽  
Fengna Li ◽  
Hongkui Wei ◽  
...  
Keyword(s):  
Amino Acid ◽  
Recent Advances ◽  
Amino Acid Sensing

Recent advances in amino acid sensing and new challenges for protein nutrition in aquaculture

2019 ◽  
Vol 1 (1) ◽  
pp. 50-59 ◽  
Author(s):  
Chengdong Liu ◽  
Xuan Wang ◽  
Huihui Zhou ◽  
Kangsen Mai ◽  
Gen He
Keyword(s):  
Amino Acid ◽  
Protein Nutrition ◽  
Recent Advances ◽  
New Challenges ◽  
Amino Acid Sensing

scholarly journals N-Carbamylglutamate and l-Arginine Promote Intestinal Absorption of Amino Acids by Regulating the mTOR Signaling Pathway and Amino Acid and Peptide Transporters in Suckling Lambs with Intrauterine Growth Restriction

2019 ◽  
Vol 149 (6) ◽  
pp. 923-932 ◽  
Author(s):  
Hao Zhang ◽  
Along Peng ◽  
Yin Yu ◽  
Shuang Guo ◽  
Mengzhi Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Signaling Pathway ◽  
Intrauterine Growth Restriction ◽  
Nutrient Absorption ◽  
Mtor Signaling ◽  
Growth Restriction ◽  
Peptide Transporter ◽  
Mtor Signaling Pathway ◽  
Intrauterine Growth ◽  
Peptide Transporters

ABSTRACT Background Previous studies have revealed that dietary N-carbamylglutamate (NCG) and l-arginine (Arg) improve intestinal integrity, oxidative state, and immune function in Hu suckling lambs with intrauterine growth restriction (IUGR). Whether these treatments alter intestinal nutrient absorption is unknown. Objective The aim of this study was to determine the influence of dietary NCG and Arg treatment during the suckling period on intestinal amino acid (AA) absorption, alterations in the mechanistic target of rapamycin (mTOR) signaling pathway, and the abundance of AA and peptide transporters in IUGR lambs. Methods On day 7 after birth, 48 newborn Hu lambs were selected from a cohort of 424 twin lambs. Normal-birth-weight and IUGR Hu lambs were allocated randomly (n = 12/group) to a control (4.09 ± 0.12 kg), IUGR (3.52 ± 0.09 kg), IUGR + 0.1% NCG (3.49 ± 0.11 kg), or IUGR + 1% Arg (3.53 ± 0.10 kg). Results At day 28, compared with the IUGR group, the IUGR groups receiving NCG and Arg had 7.4% and 7.2% greater (P < 0.05) body weight, respectively. Compared with the IUGR group, the serum concentration of insulin was greater (P < 0.05) and the cortisol was lower (P < 0.05) in the IUGR groups receiving NCG and Arg. Compared with the IUGR group, the IUGR groups receiving NCG and Arg had 13.2%–62.6% greater (P < 0.05) serum concentrations of arginine, cysteine, isoleucine, and proline. Dietary NCG or Arg to IUGR lambs resulted in greater protein abundance (P < 0.05) of peptide transporter 1 (41.9% or 38.2%) in the ileum compared with the unsupplemented IUGR lambs, respectively. Furthermore, dietary NCG or Arg treatment normalized the IUGR-induced variation (P < 0.05) in the ileal ratio of phosphorylated mTOR to total mTOR protein. Conclusion Both NCG and Arg can help mitigate the negative effect of IUGR on nutrient absorption in neonatal lambs.

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