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
AUTHORS (4)
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
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