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Trehalose‐6‐phosphate, a new regulator of yeast glycolysis that inhibits hexokinases
Sugar transport in Saccharomyces cerevisiae.
- R. Lagunas
- BiologyFEMS microbiology reviews
It is argued that there are several additional transporters for glucose that have not yet been identified that act by a facilitated diffusion mechanism and are unknown at present.
Catabolite inactivation of the glucose transport system in Saccharomyces cerevisiae.
It is concluded that the glucose transport system in S. cerevisiae is regulated by a catabolite-inactivation process that is related to the occurrence of the Pasteur effect.
Catabolite inactivation of the yeast maltose transporter occurs in the vacuole after internalization by endocytosis
It is shown that degradation of this transporter requires internalization by endocytosis and raised the question of whether in the absence of Sec18p activity the internalized maltose transporter is recycled back to the plasma membrane.
Role of phosphate in the regulation of the Pasteur effect in Saccharomyces cerevisiae.
It is concluded that, with the available data, only phosphate may be considered as a regulator of the Pasteur effect in this microorganism.
Reduced pyridine-nucleotides balance in glucose-growing Saccharomyces cerevisiae.
The results suggest that the oxidative hexose monophosphate pathway accounts for all, or almost all, the cellular requirements for NADPH and that the reoxidation of NADH is effected for a part by the respiratory chain but mainly by enzymatic reactions coupled to the reduction of organic compounds like acetaldehyde or dihydroxyacetone phosphate.
Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npi1/rsp5 and ubiquitin-hydrolase npi2/doa4.
It is shown that mutants deficient in npi1/rsp5 ubiquitin-protein ligase and npi2/doa4 ubiquitIn-protein hydrolase are required for normal endocytosis and degradation of the transporter, and that both enzymes act in the internalization step of endocyTosis.
In vivo activation of the yeast plasma membrane ATPase during nitrogen starvation Identification of the regulatory domain that controls activation
Mechanisms of appearance of the Pasteur effect in Saccharomyces cerevisiae: inactivation of sugar transport systems
The results suggest that a shift to anaerobiosis would have much greater energetic consequences in resting than in growing S. cerevisiae, and would strongly decrease the formation of ATP; as a consequence, various regulatory mechanisms would switch on, producing the observed increase of the rate of glycolysis.