Activity-dependent Reversible Inactivation of the General Amino Acid Permease
نویسندگان
چکیده
منابع مشابه
Transport Activity Dependent Regulation of the Yeast General Amino Acid Permease
The general amino acid permease Gap1p of Saccharomyces cerevisiae scavenges amino acids from the extracellular medium for use as nitrogen sources in starvation conditions. Because unlimited uptake of both naturally occurring amino acids and amino acid analogs is toxic, Gap1p is active at the plasma membrane only when amino acid levels are low. Gap1p is down regulated when amino acids are abunda...
متن کاملTransport activity–dependent intracellular sorting of the yeast general amino acid permease
Intracellular trafficking of the general amino acid permease, Gap1p, of Saccharomyces cerevisiae is regulated by amino acid abundance. When amino acids are scarce Gap1p is sorted to the plasma membrane, whereas when amino acids are abundant Gap1p is sorted from the trans-Golgi through the multivesicular endosome (MVE) and to the vacuole. Here we test the hypothesis that Gap1p itself is the sens...
متن کاملAmino Acids Regulate the Transcription , Internal Sorting , and Intrinsic Activity of the General Amino Acid Permease
The activity of the general amino acid permease in S. cerevisiae, Gap lp, is tightly regulated by amino acids through intracellular sorting as well as transport dependent inactivation at the plasma membrane. Here, we show that the two GATA type transcription factors responsible for GAPI transcription also respond to unique physiological amino acid inputs: Nillp/Gatlp activity is repressed by el...
متن کاملAmino acids regulate the intracellular trafficking of the general amino acid permease of Saccharomycescerevisiae.
The delivery to the plasma membrane of the general amino acid permease, Gap1p, of Saccharomyces cerevisiae is regulated by the quality of the nitrogen source in the growth medium. In an effort to define how different nitrogen sources control Gap1p sorting, we find that mutations in GDH1 and GLN1 that decrease the flux through the glutamate and glutamine synthesis pathways result in increased Ga...
متن کاملCharacterization of 2-aminoisobutyric acid transport in Neurospora crassa: a general amino acid permease-specific substrate.
We report the characterization of an amino acid 2-aminoisobutyric acid was transported solely by the general amino acid permease and not by the neutral amino acid permease. Furthermore, this substrate was not metabolized after transport. The potential for a system-specific nonmetabolizable substrate as a tool in the analysis of amino acid transport and its regulation is discussed.
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ژورنال
عنوان ژورنال: Molecular Biology of the Cell
سال: 2006
ISSN: 1059-1524,1939-4586
DOI: 10.1091/mbc.e06-06-0506