pH‐mediated activation of the lysosomal arginine sensor SLC38A9
FEBS Letters, EarlyView.Cells monitor nutrient levels via the lysosomal transporter SLC38A9 to activate the mechanistic target of rapamycin complex 1 (mTORC1). This study reveals that SLC38A9 function is regulated by pH. We identified histidine 544 as a critical pH sensor that undergoes conformational changes to control amino acid efflux from lysosomes; therefore, it ...
Xuelang Mu, Ampon Sae Her, Tamir Gonen
wiley +1 more source
Substrate specificity and structural investigation into PepO and PepW : two peptidases from Lactobacillus rhamnosus : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry at Massey University, Palmerston North, New Zealand [PDF]
, 2005 The proteolytic systems of lactic acid bacteria have important roles in the maturation and flavour development of cheese. Lactic acid bacteria pepetidases contribute to the taste of cheese through the production of low-molecular weight peptides and free ...
Yates, Karen Maree
core
The Arabidopsis NLP7 gene regulates nitrate signaling via NRT1.1-dependent pathway in the presence of ammonium. [PDF]
, 2018 Nitrate is not only an important nutrient but also a signaling molecule for plants. A few of key molecular components involved in primary nitrate responses have been identified mainly by forward and reverse genetics as well as systems biology, however ...
Crawford, Nigel M +7 more
core +1 more source
Molecular Oncology, EarlyView.Meta‐transcriptome analysis identified FGF19 as a peptide enteroendocrine hormone associated with colorectal cancer prognosis. In vivo xenograft models showed release of FGF19 into the blood at levels that correlated with tumor volumes. Tumoral‐FGF19 altered murine liver metabolism through FGFR4, thereby reducing bile acid synthesis and increasing ...
Jordan M. Beardsley +5 more
wiley +1 more source
The effect of amino acid deprivation on the transfer of iron through Caco-2 cell monolayers [PDF]
, 2017 Funding Source Rural and Environmental Scientific and Analytical Services, the Scottish Government Acknowledgments We thank Dr Helen Hayes for her technical support during this project.
Cottin, Sarah +3 more
core +3 more sources
Renal transport of neutral amino acids. Tubular localization of Na+-dependent phenylalanine- and glucose-transport systems [PDF]
Biochemical Journal, 1984 The transport properties for phenylalanine and glucose in luminal-membrane vesicles from outer cortex (pars convoluta) and outer medulla (pars recta) of rabbit kidney were studied by a spectrophotometric method. Uptake of phenylalanine as well as of glucose by the two types of membrane vesicles was found to be Na+-dependent, electrogenic and ...
U, Kragh-Hansen +3 more
openaire +2 more sources
Molecular Oncology, EarlyView.This work identified serum proteins associated with pancreatic epithelial neoplasms (PanINs) and early‐stage PDAC. Proteomics screens assessed genetically engineered mice with abundant PanINs, KPC mice (Lox‐STOP‐Lox‐KrasG12D/+ Lox‐STOP‐Lox‐Trp53R172H/+ Pdx1‐Cre) before PDAC development and also early‐stage PDAC patients (n = 31), compared to benign ...
Hannah Mearns +10 more
wiley +1 more source
Diel rhythmicity in amino acid uptake by Prochlorococcus [PDF]
, 2008 The marine cyanobacterium Prochlorococcus, the most abundant phototrophic organism on Earth, numerically dominates the phytoplankton in nitrogen (N)-depleted oceanic gyres.
Burkill, Peter H. +7 more
core +3 more sources
Neutral amino acid transport systems in Chinese hamster ovary cells.
Journal of Biological Chemistry, 1981 The neutral amino acid transport systems A, ASC, and L have been characterized in the Chinese hamster ovary cell. System A, defined by its sodium ion dependency and inhibition by 2-methylaminoisobutyric acid, was found to be extremely sensitive to the pH of the external medium and to increase in response to starvation for amino acids.
M A, Shotwell +3 more
openaire +2 more sources
Characterization of the amino acid response element within the human sodium-coupled neutral amino acid transporter 2 (SNAT2) System A transporter gene [PDF]
Biochemical Journal, 2006 The neutral amino acid transport activity, System A, is enhanced by amino acid limitation of mammalian cells. Of the three gene products that encode System A activity, the one that exhibits this regulation is SNAT2 (sodium-coupled neutral amino acid transporter 2). Fibroblasts that are deficient in the amino acid response pathway exhibited little or no
Stela S, Palii +4 more
openaire +2 more sources