TY - JOUR
T1 - A Plasma Membrane Association Module in Yeast Amino Acid Transporters
AU - Popov-Čeleketić, Dušan
AU - Bianchi, Frans
AU - Ruiz, Stephanie J
AU - Meutiawati, Febrina
AU - Poolman, Bert
N1 - Copyright © 2016, The American Society for Biochemistry and Molecular Biology.
PY - 2016/7/29
Y1 - 2016/7/29
N2 - 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 found 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 an amphipathic alpha-helix and the FWC signature, which is palmitoylated by palmitoyltransferase 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.
AB - 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 found 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 an amphipathic alpha-helix and the FWC signature, which is palmitoylated by palmitoyltransferase 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.
KW - PROTEIN SECONDARY STRUCTURE
KW - NUCLEAR-PORE COMPLEX
KW - KINASE-A PATHWAY
KW - SACCHAROMYCES-CEREVISIAE
KW - PHEROMONE RESPONSE
KW - MASTER REGULATOR
KW - GENE-EXPRESSION
KW - CELL-SURFACE
KW - CORTICAL ER
KW - PERMEASE
U2 - 10.1074/jbc.M115.706770
DO - 10.1074/jbc.M115.706770
M3 - Article
C2 - 27226538
SN - 0021-9258
VL - 291
SP - 16024
EP - 16037
JO - The Journal of Biological Chemistry
JF - The Journal of Biological Chemistry
IS - 31
ER -