A plasma membrane association module in yeast amino acid transporters.
SourceJournal of Biological Chemistry, 291, 31, (2016), pp. 16024-37
Article / Letter to editor
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Journal of Biological Chemistry
SubjectRadboudumc 11: Renal disorders RIMLS: Radboud Institute for Molecular Life Sciences
Amino acid permeases (AAPs) in the plasma membrane (PM) of Saccharomyces cerevisiae are responsible for the uptake of amino acids and involved in regulation of their cellular levels. Here, we report on a strong and complex module for PM association found in the C-terminal tail of AAPs. Using in silico analyses and mutational studies we find that the C-terminal sequences of Gap1, Bap2, Hip1, Tat1, Tat2, Mmp1, Sam3, Agp1, and Gnp1 are about 50 residues long, associate with the PM and have features that discriminate them from the termini of organellar amino acid transporters. We show that this sequence (named PMasseq) contains a amphipathic alpha-helix and the FWC signature, which is palmitoylated by palmitoyl transferase Pfa4. Variations of PMasseq, found in different AAPs, lead to different mobilities and localization patterns, whereas the disruption of the sequence has an adverse effect on cell viability. We propose that PMasseq modulates the function and localization of AAPs along the PM. PMasseq is one of the most complex protein signals for plasma membrane association across species, and can be used as a delivery vehicle for the PM.
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