title: Pil1, an eisosome organizer, plays an important role in the recruitment of synaptojanins and amphiphysins to facilitate receptor-mediated endocytosis in yeast.
abstract: The eisosome protein Pil1 is known to be implicated in the endocytosis of Ste3, but the precise biological function of it during endocytosis is poorly understood. Here, we present data to reveal Pil1's role in receptor-mediated endocytosis. Using live cell imaging, we show that endocytic patches carrying Abp1 and Las17 persisted much longer in PIL1-deficient cells. The loss of Pil1 also greatly affected both the scission efficiency and the frequency of formation of endocytic sites carrying Rvs161- and Rvs167-GFP. Furthermore, the mistargeting of the synaptojanins, Sjl1 and Sjl2, to the cytoplasm in pil1Δ cells suggests that Pil1 is required for the proper recruitment of the synaptojanins to endocytic sites. A severe motility defect of Abp1-GFP during its internalization in a codeletant of PIL1 and SJL2 indicates a functional interplay between them in endocytosis. Together, these results establish that Pil1 is involved in the recruitment of endocytic proteins to optimize endocytosis.
authors.affiliation: Department of Biology, Missouri State University, 901 South National Ave., Springfield, MO 65897, USA.
authors.forename: Erin R
authors.initials: ER
authors.lastname: Murphy
authors.forename: Jacob
authors.initials: J
authors.lastname: Boxberger
authors.forename: Robert
authors.initials: R
authors.lastname: Colvin
authors.forename: Suk Je
authors.initials: SJ
authors.lastname: Lee
authors.forename: Geoffrey
authors.initials: G
authors.lastname: Zahn
authors.forename: Fred
authors.initials: F
authors.lastname: Loor
authors.forename: Kyoungtae
authors.initials: K
authors.lastname: Kim
mesh_terms: D000199:Actins / Q000378:metabolism; D021961:Cell Membrane Structures / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D004705:Endocytosis; D017353:Gene Deletion; D055786:Gene Knockout Techniques; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism; D010590:Phalloidine / Q000378:metabolism; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D000097573:Red Fluorescent Protein
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins; D008840:Microfilament Proteins; D010590:Phalloidine; D010750:Phosphoproteins; D010744:Phosphoric Monoester Hydrolases; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D000097573:Red Fluorescent Protein; C487327:PIL1 protein, S cerevisiae; C089181:RVS161 protein, S cerevisiae; C082282:RVS167 protein, S cerevisiae; C110551:INP51 protein, S cerevisiae; C110552:INP52 protein, S cerevisiae