title: A role for eisosomes in maintenance of plasma membrane phosphoinositide levels.
abstract: The plasma membrane delineates the cell and mediates its communication and material exchange with the environment. Many processes of the plasma membrane occur through interactions of proteins with phosphatidylinositol(4,5)-bisphosphate (PI(4,5)P2), which is highly enriched in this membrane and is a key determinant of its identity. Eisosomes function in lateral organization of the plasma membrane, but the molecular function of their major protein subunits, the BAR domain-containing proteins Pil1 and Lsp1, is poorly understood. Here we show that eisosomes interact with the PI(4,5)P2 phosphatase Inp51/Sjl1, thereby recruiting it to the plasma membrane. Pil1 is essential for plasma membrane localization and function of Inp51 but not for the homologous phosphatidylinositol bisphosphate phosphatases Inp52/Sjl2 and Inp53/Sjl3. Consistent with this, absence of Pil1 increases total and available PI(4,5)P2 levels at the plasma membrane. On the basis of these findings, we propose a model in which the eisosomes function in maintaining PI(4,5)P2 levels by Inp51/Sjl1 recruitment.
authors: Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510 Department of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115 twalther@hsph.harvard.edu froehlic@hsph.harvard.edu.
authors: Florian
authors: F
authors: Fröhlich
authors: Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510 Department of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115.
authors: Romain
authors: R
authors: Christiano
authors: Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510 Department of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115.
authors: Daniel K
authors: DK
authors: Olson
authors: Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510 Howard Hughes Medical Institute and Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale School of Medicine, New Haven, CT 06510.
authors: Abel
authors: A
authors: Alcazar-Roman
authors: Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510 Howard Hughes Medical Institute and Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale School of Medicine, New Haven, CT 06510.
authors: Pietro
authors: P
authors: DeCamilli
authors: Department of Cell Biology, Yale School of Medicine, New Haven, CT 06510 Department of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115 Department of Cell Biology, Harvard Medical School, Boston, MA 02115 twalther@hsph.harvard.edu froehlic@hsph.harvard.edu.
authors: Tobias C
authors: TC
authors: Walther
mesh_terms: D002462:Cell Membrane; D015388:Organelles / Q000201:enzymology* / Q000502:physiology; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism*; D010750:Phosphoproteins / Q000502:physiology; D010744:Phosphoric Monoester Hydrolases / Q000502:physiology; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology
chemical_list: C487327:PIL1 protein, S cerevisiae; D019269:Phosphatidylinositol 4,5-Diphosphate; D010750:Phosphoproteins; D029701:Saccharomyces cerevisiae Proteins; C110551:INP51 protein, S cerevisiae; C110552:INP52 protein, S cerevisiae; C110553:INP53 protein, S cerevisiae; D010744:Phosphoric Monoester Hydrolases