Document Type
Article
Publication Date
8-31-2011
Publication Title
Molecular Biology of the Cell
Department
Geisel School of Medicine
Abstract
The cortical cytoskeleton mediates a range of cellular activities such as endocytosis, cell motility, and the maintenance of cell rigidity. Traditional polymers, including actin, microtubules, and septins, contribute to the cortical cytoskeleton, but additional filament systems may also exist. In yeast cells, cortical structures called eisosomes generate specialized domains termed MCCs to cluster specific proteins at sites of membrane invaginations. Here we show that the core eisosome protein Pil1 forms linear cortical filaments in fission yeast cells and that purified Pil1 assembles into filaments in vitro. In cells, Pil1 cortical filaments are excluded from regions of cell growth and are independent of the actin and microtubule cytoskeletons. Pil1 filaments assemble slowly at the cell cortex and appear stable by time-lapse microscopy and fluorescence recovery after photobleaching. This stability does not require the cell wall, but Pil1 and the transmembrane protein Fhn1 colocalize and are interdependent for localization to cortical filaments. Increased Pil1 expression leads to cytoplasmic Pil1 rods that are stable and span the length of cylindrical fission yeast cells. We propose that Pil1 is a novel component of the yeast cytoskeleton, with implications for the role of filament assembly in the spatial organization of cells.
DOI
10.1091/mbc.E11-07-0605
Original Citation
Kabeche R, Baldissard S, Hammond J, Howard L, Moseley JB. The filament-forming protein Pil1 assembles linear eisosomes in fission yeast. Mol Biol Cell. 2011 Nov;22(21):4059-67. doi: 10.1091/mbc.E11-07-0605. Epub 2011 Sep 7. PMID: 21900489; PMCID: PMC3204068.
Dartmouth Digital Commons Citation
Kabeche, Ruth; Baldissard, Suzanne; Hammond, John; Howard, Louisa; and Moseley, James B., "The Filament-Forming Protein Pil1 Assembles Linear Eisosomes in Fission Yeast" (2011). Dartmouth Scholarship. 3870.
https://digitalcommons.dartmouth.edu/facoa/3870