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

Recent advances in amino acid analysis by capillary electromigration methods: June 2015-May 2017

2017 ◽  
Vol 39 (1) ◽  
pp. 190-208 ◽  
Author(s):  
Véréna Poinsot ◽  
Varravaddheay Ong-Meang ◽  
Audrey Ric ◽  
Pierre Gavard ◽  
Lucie Perquis ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Recent Advances

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.

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