Activity-dependent Reversible Inactivation of the General Amino Acid Permease

Enzyme Activation Protein Transport 0303 health sciences 03 medical and health sciences Saccharomyces cerevisiae Proteins Amino Acid Transport Systems Gene Expression Regulation, Fungal Cell Membrane Saccharomyces cerevisiae Amino Acids Enzyme Inhibitors
DOI: 10.1091/mbc.e06-06-0506 Publication Date: 2006-08-03T00:53:08Z
ABSTRACT
The general amino acid permease, Gap1p, of Saccharomyces cerevisiae transports all naturally occurring acids into yeast cells for use as a nitrogen source. Previous studies have shown that nonubiquitinateable form the Gap1p(K9R,K16R), is constitutively localized to plasma membrane. Here, we report transport activity Gap1p(K9R,K16R) can be rapidly and reversibly inactivated at membrane by presence mixtures. Surprisingly, also find addition most single lethal Gap1p(K9R,K16R)-expressing cells, whereas mixtures are less toxic. This toxicity appears consequence uptake unusually large quantities acid. Exploiting this toxicity, isolated gap1 alleles deficient in subset acids. Using these mutations, show Gap1p inactivation does not depend on either extracellular or intracellular acids, but require active Gap1p. Together, our findings uncover new mechanism inhibition permease response elevated levels provide physiological explanation stringent regulation
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (39)
CITATIONS (56)
EXTERNAL LINKS
PlumX Metrics
RECOMMENDATIONS
FAIR ASSESSMENT
Coming soon ....
JUPYTER LAB
Coming soon ....