Yeast nutrient transceptors provide novel insight in the functionality of membrane transporters

In the yeast Saccharomyces cerevisiae several nutrient transporters have been identified that possess an additional function as nutrient receptor. These transporters are induced when yeast cells are starved for their substrate, which triggers entry into stationary phase and acquirement of a low prot...

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Vydáno v:	Current genetics Ročník 59; číslo 4; s. 197 - 206
Hlavní autoři:	Schothorst, Joep, Kankipati, Harish Nag, Conrad, Michaela, Samyn, Dieter R, Van Zeebroeck, Griet, Popova, Yulia, Rubio-Texeira, Marta, Persson, Bengt L, Thevelein, Johan M
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Berlin/Heidelberg Springer-Verlag 01.11.2013 Springer Berlin Heidelberg Springer Nature B.V
Témata:	agonists Amino Acid Sequence Amino Acid Transport Systems Amino Acid Transport Systems - metabolism Amino acids Biochemistry Biokemi Biomedical and Life Sciences cAMP-dependent protein kinase Cell Biology chemistry Cyclic AMP-Dependent Protein Kinases Cyclic AMP-Dependent Protein Kinases - metabolism endocytosis Endocytosis - physiology genetics Inactivation ions Life Sciences Membrane Transport Proteins Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism metabolism Microbial Genetics and Genomics Microbiology Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Nutrients phenotype Phosphates Phosphates - chemistry Phosphates - metabolism physiology Plant Sciences Protein Conformation Proteomics Research Article Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Proteins - metabolism Signal Transduction Signal Transduction - physiology site-directed mutagenesis Sodium Sodium - metabolism symporters Ubiquitination vacuoles Yeasts Endocytosis Ubiquitination Proton binding Nutrient signaling Co-transport Transceptor
ISSN:	0172-8083, 1432-0983, 1432-0983
On-line přístup:	Získat plný text
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Shrnutí:	In the yeast Saccharomyces cerevisiae several nutrient transporters have been identified that possess an additional function as nutrient receptor. These transporters are induced when yeast cells are starved for their substrate, which triggers entry into stationary phase and acquirement of a low protein kinase A (PKA) phenotype. Re-addition of the lacking nutrient triggers exit from stationary phase and sudden activation of the PKA pathway, the latter being mediated by the nutrient transceptors. At the same time, the transceptors are ubiquitinated, endocytosed and sorted to the vacuole for breakdown. Investigation of the signaling function of the transceptors has provided a new read-out and new tools for gaining insight into the functionality of transporters. Identification of amino acid residues that bind co-transported ions in symporters has been challenging because the inactivation of transport by site-directed mutagenesis is not conclusive with respect to the cause of the inactivation. The discovery of nontransported agonists of the signaling function in transceptors has shown that transport is not required for signaling. Inactivation of transport with maintenance of signaling in transceptors supports that a true proton-binding residue was mutagenised. Determining the relationship between transport and induction of endocytosis has also been challenging, since inactivation of transport by mutagenesis easily causes loss of all affinity for the substrate. The use of analogues with different combinations of transport and signaling capacities has revealed that transport, ubiquitination and endocytosis can be uncoupled in several unexpected ways. The results obtained are consistent with transporters undergoing multiple substrate-induced conformational changes, which allow interaction with different accessory proteins to trigger specific downstream events.
Bibliografie:	http://dx.doi.org/10.1007/s00294-013-0413-y ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 Communicated by H. Sychrova.
ISSN:	0172-8083 1432-0983 1432-0983
DOI:	10.1007/s00294-013-0413-y