Title : Structural and physiologic determinants of human erythrocyte sugar transport regulation by adenosine triphosphate.

Pub. Date : 1998 Sep 1

PMID : 9724536






13 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 (1) Where is the GLUT1 ATP binding site? Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
2 GLUT1 residues 301-364 were identified as one element of the GLUT1 ATP binding domain by peptide mapping and N-terminal sequence analysis of proteolytic fragments of azidoATP-photolabeled GLUT1. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
3 GLUT1 residues 301-364 were identified as one element of the GLUT1 ATP binding domain by peptide mapping and N-terminal sequence analysis of proteolytic fragments of azidoATP-photolabeled GLUT1. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
4 GLUT1 residues 301-364 were identified as one element of the GLUT1 ATP binding domain by peptide mapping and N-terminal sequence analysis of proteolytic fragments of azidoATP-photolabeled GLUT1. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
5 Nucleotide binding and sugar transport experiments undertaken with dimeric and tetrameric forms of GLUT1 indicate that only tetrameric GLUT1 binds and is subject to modulation by ATP. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
6 Nucleotide binding and sugar transport experiments undertaken with dimeric and tetrameric forms of GLUT1 indicate that only tetrameric GLUT1 binds and is subject to modulation by ATP. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
7 Reconstitution experiments indicate that nucleotide and tetrameric GLUT1 are sufficient for ATP modulation of sugar transport. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
8 Feedback control of GLUT1 regulation by ATP was investigated by measuring sugar uptake into erythrocyte ghosts containing or lacking ATP and glycolytic intermediates. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
9 Feedback control of GLUT1 regulation by ATP was investigated by measuring sugar uptake into erythrocyte ghosts containing or lacking ATP and glycolytic intermediates. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
10 Reduced cytosolic pH inhibits ATP modulation of GLUT1-mediated 3OMG uptake and increases Kd(app) for ATP interaction with GLUT1. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
11 Reduced cytosolic pH inhibits ATP modulation of GLUT1-mediated 3OMG uptake and increases Kd(app) for ATP interaction with GLUT1. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
12 Reduced cytosolic pH inhibits ATP modulation of GLUT1-mediated 3OMG uptake and increases Kd(app) for ATP interaction with GLUT1. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens
13 We conclude that tetrameric but not dimeric GLUT1 is subject to direct regulation by cytosolic ATP and that this regulation is antagonized by intracellular AMP and acidification. Adenosine Triphosphate solute carrier family 2 member 1 Homo sapiens