scholarly journals The yeast Aft2 transcription factor determines selenite toxicity by controlling the low affinity phosphate transport system

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
María Pérez-Sampietro ◽  
Albert Serra-Cardona ◽  
David Canadell ◽  
Celia Casas ◽  
Joaquín Ariño ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transport System ◽  
Phosphate Transport ◽  
Selenite Toxicity

scholarly journals RCO-3 and COL-26 form an external-to-internal module that regulates the dual-affinity glucose transport system in Neurospora crassa

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Jinyang Li ◽  
Qian Liu ◽  
Jingen Li ◽  
Liangcai Lin ◽  
Xiaolin Li ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Neurospora Crassa ◽  
Glucose Transport ◽  
Transport System ◽  
Rational Design ◽  
Glucose Sensor ◽  
Glucose Transporters ◽  
Glucose Fluctuation ◽  
High Affinity ◽  
Glucose Transport System

Abstract Background Low- and high-affinity glucose transport system is a conserved strategy of microorganism to cope with environmental glucose fluctuation for their growth and competitiveness. In Neurospora crassa, the dual-affinity glucose transport system consists of a low-affinity glucose transporter GLT-1 and two high-affinity glucose transporters HGT-1/HGT-2, which play diverse roles in glucose transport, carbon metabolism, and cellulase expression regulation. However, the regulation of this dual-transporter system in response to environmental glucose fluctuation is not yet clear. Results In this study, we report that a regulation module consisting of a downstream transcription factor COL-26 and an upstream non-transporting glucose sensor RCO-3 regulates the dual-affinity glucose transport system in N. crassa. COL-26 directly binds to the promoter regions of glt-1, hgt-1, and hgt-2, whereas RCO-3 is an upstream factor of the module whose deletion mutant resembles the Δcol-26 mutant phenotypically. Transcriptional profiling analysis revealed that Δcol-26 and Δrco-3 mutants had similar transcriptional profiles, and both mutants had impaired response to a glucose gradient. We also showed that the AMP-activated protein kinase (AMPK) complex is involved in regulation of the glucose transporters. AMPK is required for repression of glt-1 expression in starvation conditions by inhibiting the activity of RCO-3. Conclusions RCO-3 and COL-26 form an external-to-internal module that regulates the glucose dual-affinity transport system. Transcription factor COL-26 was identified as the key regulator. AMPK was also involved in the regulation of the dual-transporter system. Our findings provide novel insight into the molecular basis of glucose uptake and signaling in filamentous fungi, which may aid in the rational design of fungal strains for industrial purposes.

Establishment of a Parathyroid Hormone-Responsive Phosphate Transport System in Vitro Using Cultured Renal Cells*

Endocrinology ◽  
1986 ◽  
Vol 119 (5) ◽  
pp. 1954-1963 ◽  
Author(s):  
YOSHIKAZU KINOSHITA ◽  
MASAAKI FUKASE ◽  
AKIMITSU MIYAUCHI ◽  
MUTSUMI TAKENAKA ◽  
MASAKI NAKADA ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Transport System ◽  
Phosphate Transport ◽  
Renal Cells

Phosphate uptake by renal membrane vesicles of rabbits adapted to high and low phosphorus diets

1983 ◽  
Vol 245 (2) ◽  
pp. F175-F180 ◽  
Author(s):  
L. Cheng ◽  
C. T. Liang ◽  
B. Sacktor
Keyword(s):  
Transport System ◽  
Phosphate Uptake ◽  
Membrane Vesicles ◽  
Phosphate Transport ◽  
Uptake System ◽  
Low Phosphorus ◽  
Dietary Phosphate ◽  
Preferred Species ◽  
Uptake Medium ◽  
Phosphate Carrier

Renal adaptation to changes in phosphate intake was studied by comparing phosphate uptake by proximal tubule brush border membrane vesicles from rabbits on a relatively high or low phosphorus diet. The low phosphorus diet increased Na+ gradient-dependent phosphate uptake. Uptake in the absence of Na+ and in the presence of Na+, but no gradient, was not significantly affected. The phosphorus diet did not alter Na+ gradient-dependent D-glucose and L-proline uptake. The low phosphorus diet increased Vmax; affinity for phosphate was not appreciably changed. At all concentrations of extravesicular Na+, phosphate uptake was higher in membrane vesicles from animals fed the low phosphorus diet; the kinetics of the phosphate uptake system, with respect to Na+, was also altered by the change in dietary phosphate. These findings suggest that adaptation involves an alteration in the rate of translocation of the Na+-phosphate carrier when energized by a Na+ gradient driving force rather than a change in the number of Na+-phosphate carrier sites. With membrane vesicles from rabbits fed a low phosphorus diet, phosphate uptake increased several-fold when the pH of the uptake medium was raised, whereas with membrane vesicles from animals fed a high phosphorus diet the enhancement of uptake with alkalinization was relatively small. Irrespective of the diet, divalent phosphate was the probable preferred species for transport. Dietary adaptation was associated, however, with an alteration in the pH dependency of the transport system per se. These findings provide evidence that the adaptation of the kidney phosphate transport system to dietary phosphate load involves an intrinsic change in the Na+-phosphate carrier.

On the involvement of a glucose 6-phosphate transport system in the function of microsomal glucose 6-phosphatase

1975 ◽  
Vol 6 (2) ◽  
pp. 75-83 ◽  
Author(s):  
William J. Arion ◽  
Bruce K. Wallin ◽  
Alex J. Lange ◽  
Lawrence M. Ballas
Keyword(s):  
Transport System ◽  
Phosphate Transport

scholarly journals The Protein Component(s) of the Isolated Phosphate-Transport System of Mitochondria

2005 ◽  
Vol 128 (1) ◽  
pp. 97-105 ◽  
Author(s):  
Hanno V. J. KOLBE ◽  
Peter MENDE ◽  
Bernhard KADENBACH
Keyword(s):  
Transport System ◽  
Phosphate Transport ◽  
Protein Component
Sign in / Sign up

Export Citation Format

Share Document