Transport and transport-associated phosphorylation of 2-deoxy-d-glucose in yeast

Steveninck, J. Van

doi:10.1016/0005-2736(68)90123-5

Cited by 111 publications

(41 citation statements)

References 23 publications

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“…The phosphory1ation-dephosphorylation hypothesis originally proposed to account for active glucose absorption in mammalian intestine was abandoned as a result of more recent evidence (see Crane, 1960 for a review). Phosphory1ation-linked sugar transport, however, has been demonstrated in bacteria (Simoni et a1., 1967;Kaback, 1968) and yeast (van Steveninck, 1968(van Steveninck, , 1969(van Steveninck, , 1970(van Steveninck, , 1972Jaspers & van Steveninck, 1975). The present finding of the accumulation of phosphorylated compounds in crustacean midgut cannot be taken as conclusive evidence for this hypothesis since many cells increase the concentration of metabolic intermediates on the supply of nutrients.…”

Section: Discussioncontrasting

confidence: 43%

Sodium and glucose transport across the in vitro perfused midgut of the blue crab, Callinectes sapidus Rathbun

Chu¹

1984

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Section: Discussioncontrasting

confidence: 43%

Sodium and glucose transport across the in vitro perfused midgut of the blue crab, Callinectes sapidus Rathbun

Chu¹

1984

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“…Although a small fraction is phosphorylated [32], glucose, with IAA present, exists in the cell largely as the free sugar [5], able, therefore, to compete with sorbose for transport at the compartment membrane. DOG exists in both phosphorylated and free form; at a 10 mM external concentration, enough free sugar should be present inside the cell [31] to compete effectively with sorbose. DOG does not eliminate the slow component of efflux (see Fig.…”

Section: Discussionmentioning

confidence: 99%

Reversible permeability changes in the membrane of a yeast cell sugar compartment

et al. 1975

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Sorbose uptake by Saccharomyces cerevisiae was increased 40 to 60% by glucose and other metabolizable sugars. Neither growth nor binding accounted for the increased uptake. However, accessibility of a restrictive intracellular compartment was increased as shown by counterflow and efflux measurements. Efflux from the compartment was more than doubled by glucose. This effect was reversed by washing and was prevented by iodoacetic acid and other inhibitors, but not by cycloheximide. No evidence was found for a facilitated transport system in the compartment membrane such as exists in the external cell membrane. It was concluded that sorbose crosses the compartment membrane by simple diffusion and that a reaction requiring the metabolism of sugars increases the permeability of the membrane. Arabinose and fucose entered and were lost from the compartment like sorbose, whereas dimethylsulfoxide was unaffected by the compartment. All three of these later compounds were bound by the cells when glucose was available in uptake suspensions. Binding was prevented by iodoacetic acid, but not by cycloheximide.

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“…The situation at the sugar transport step is complicated by the evidence for coupling between sugar transport and sugar phosphorylation [22]. (In the triple mutant hxkl hxk2 glkl, glucose enters by means of facilitated diffusion [23].)…”

Section: Discussionmentioning

confidence: 99%

Studies on the mechanism of the glucose‐induced cAMP signal in glycolysis and glucose repression mutants of the yeast Saccharomyces cerevisiae

Beullens

Mbonyi

Geerts

et al. 1988

European Journal of Biochemistry

126

146

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When glucose is added to cells of the yeast Succharomyces cerevisiae grown on non-fermentable carbon sources, a cAMP signal is induced which triggers a protein phosphorylation cascade. Addition of glucose or fructose to cells of a phosphoglucose isomerase mutant also induced the cAMP signal indicating that metabolization of the sugar beyond the sugar phosphate step is not necessary. Glucose 6-phosphate might stimulate the triggering reaction since induction with fructose shows a significant delay. Experiments with double and triple mutants in hexokinase 1, hexokinase 2 or glucokinase indicated that the presence of one of the three kinases was both necessary and enough for induction of the cAMP signal by glucose and the presence of one of the two hexokinases necessary and enough for induction by fructose. The product of the kinase reaction itself however does not appear to be the trigger of the reaction: when the increase in the level of glucose 6-phosphate and fructose 6-phosphate was measured as a function of time after addition of different glucose concentrations, no correlation was observed with the increase in the cAMP level. From the dependence of the cAMP increase on the external concentration of glucose, a rough estimate was obtained of the K , of the triggering reaction: about 25 mM. This value clearly fits with the K , of the low-affinity glucose carrier (about 20 mM) and differs by at least an order of magnitude from the K , values of the high-affinity glucose carrier and the three kinases. The present results situate the primary triggering reaction at the level of transport-associated phosphorylation. The main (= low-affinity) glucose carrier appears to be the receptor while association of the corresponding kinase is needed for induction of the signal. Since it is known that the presence of the kinases influences the characteristics of sugar transport, no definite conclusion can be given on whether the necessity of the kinases reflects the need for a certain type of transport or the need for phosphorylation of the sugar. The increase in the level of fructose 1,6-bisphosphate, on the other hand, correlated very well with the cAMP increase. However, it clearly lagged behind the cAMP increase, confirming the previously suggested importance of the cAMP signal for the stimulation of glycolytic flux at the level of phosphofructokinase 1. The importance of the cAMP signal for the stimulation of phosphofructokinase 1 also provides an explanation for the transient overshoot in the levels of glucose 6-phosphate and fructose 6-phosphate which are observed after addition of glucose to derepressed yeast cells. Addition of glucose to glucoserepressed wild-type cells triggers no or just a very weak cAMP signal, indicating that one of the intermediates in the induction sequence must be glucose repressible. This conclusion was confirmed by experiments with wild-type cells grown on either galactose or maltose (which have less glucose repression) and with cells of the hxk2 mutant which is deficient in glucose repression...

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Transport and transport-associated phosphorylation of 2-deoxy-d-glucose in yeast

Cited by 111 publications

References 23 publications

Sodium and glucose transport across the in vitro perfused midgut of the blue crab, Callinectes sapidus Rathbun

Sodium and glucose transport across the in vitro perfused midgut of the blue crab, Callinectes sapidus Rathbun

Reversible permeability changes in the membrane of a yeast cell sugar compartment

Studies on the mechanism of the glucose‐induced cAMP signal in glycolysis and glucose repression mutants of the yeast Saccharomyces cerevisiae

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