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• W595607650 abstract "In the plasma membrane of cells the complex variety of components is sorted into subcompartments, microdomains and nanoclusters. We only begin to understand the principles of this higher order. The heterogeneity of these subunits creates individual microenvironments for various membrane linked processes like substrate transport, signal perception and transduction, or interaction between cells. The yeast Saccharomyces cerevisiae is a particularly suitable model organism to investigate plasma membrane compartmentation. In addition to homogenously distributed membrane proteins, two non-overlapping, stable and immobile distribution patterns exist, which can be resolved by light microscopy. This work focuses on composition, formation and stabilization of the spotty membrane compartment of the arginine permease Can1 (MCC) and provides evidence for the biological significance of protein segregation within the plasma membrane.In adult mother cells, MCC forms 40 to 60 patchy domains that can be studied by tagging MCC protein constituents with fluorescent proteins. In addition to the known members Can1, the protein of unknown function Sur7 and the uracil permease Fur4, eleven further proteins could be localized. From published localization data of other groups additional MCC located proteins could be identified, raising the total number to 21 proteins within or associated with this membrane compartment. Only nine of these proteins are transmembrane proteins, while the other twelve are attached to MCC on the cytosolic side of the plasma membrane. Not only proteins, but also membrane lipids follow this compart-mentation. By the finding that Filipin-stained sterols accumulate within MCC as well, an inhomogeneous distribution of lipids in non-polarized cells could be demonstrated for the first time. Consistently, the tryptophan transporter Tat2 was also localized within MCC when tagged with green fluorescent protein (GFP). For Tat2, a dependence of ergosterol for correct targeting to the plasma membrane had been shown previously. In contrast to the local accumulation of Tat2-GFP, the tagged amino acid permease Gap1-GFP was equally distributed in the plasma membrane under all tested conditions. Gap1 differs from Tat2 in its dependence on sphingolipids for correct conformation, transport activity and stability in the membrane. According to the potentially lipid-mediated sorting of Tat2, also the ergosterol-binding hexose/H+-symporter HUP1 from Chlorella kessleri could be localized within MCC after tagging with GFP and heterologous expression in S. cerevisiae. A detailed analysis of the association of HUP1-GFP with MCC unveiled a high dependence of the patchy distribution on the energization of the plasma membrane, which could be confirmed for all MCC located H+-symporters. As soon as the membrane potential is uncoupled by an ionophor or an electrical pulse, the transporters dissipate from the compartment. Upon repolarization the transporters again accumulate within MCC. However, this behavior was only observed for H+-symporters, while no movement was detectable for other transmembrane or associated proteins. Nevertheless, this finding demonstrates a previously unknown function of the membrane potential in the lateral organization of the plasma membrane.In addition to this physical parameter 28 genes could be identified, that are necessary for a correct MCC formation. Using HUP1-GFP as a marker protein a genome-wide, visual screen was performed, addressing all viable single-deletion mutants. Among the identified genes those were significantly overrepresented that affect lipid metabolism (especially ergosterol biosynthesis) or vesicle-mediated transport. By testing the distribution of further MCC marker proteins as well as filipin-stained sterols a group of six most severely affected mutants could be identified, including the deletion strains nce102Δ and pil1Δ. Both proteins, Nce102 and Pil1, colocalize with MCC and therefore are regulators of domain formation in situ. While Nce102 is an integral membrane protein of unknown function, the soluble Pil1 is one of the main components of eisosomes. This novel structure beneath MCC is suggested to mark sites of active endocytosis. However, own localization studies using the GFP-tagged endocytic markers Rvs161, Ede1 and Sla2 revealed a clear separation of MCC and sites of active endocytosis. Mutant analyses showed that the lack of Pil1 or Nce102 rather accelerates the substrate-induced degradation of the MCC protein Can1. Prior to internalization Can1 leaves MCC which presumably makes it available for enzymes of the endocytic machinery. In both mutants Can1 is equally distributed from the beginning, thereby shortening the initial steps of internalization. Thus, MCC forms a protective �shelter� within the plasma membrane to regulate the turnover of membrane proteins." @default.
• W595607650 created "2016-06-24" @default.
• W595607650 creator A5041506005 @default.
• W595607650 date "2009-03-15" @default.
• W595607650 modified "2023-09-26" @default.
• W595607650 title "Plasma membrane compartmentation in Saccharomyces cerevisiae" @default.
• W595607650 hasPublicationYear "2009" @default.
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