Evidence map›Paper›PMID 21900489›Full record

ArticleMolecular biology of the cell2011

The filament-forming protein Pil1 assembles linear eisosomes in fission yeast.

Ruth Kabeche, Suzanne Baldissard, John Hammond, Louisa Howard, James B Moseley

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Fission yeast Pdk1 kinase regulates cytokinesis and eisosomes.bioRxiv : the preprint server for biology · 2025
    Article
  3. The Predicted Structure ofJournal of fungi (Basel, Switzerland) · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The TOR pathway modulates cytoophidium formation inThe Journal of biological chemistry · 2019
    Article
  18. Review
  19. Article
  20. Eisosomes.Current biology : CB · 2018
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ruth KabecheDepartment of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
Suzanne Baldissard
John Hammond
Louisa Howard
James B Moseley
Dartmouth College · US

Funding

Developing Faculty Leaders in the Biomedical SciencesP30GM092357 · NIGMS · DARTMOUTH COLLEGE · PI BARLOWE, CHARLES K · 2009 to 2010
$691k
NIGMS NIH HHS P30 GM092357NIGMS NIH HHS P30GM092357
6 · The paper itself

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.

Indexed as

Apraxia, IdeomotorCell DivisionCell Membrane StructuresCell PolarityCytoskeletal ProteinsCytoskeletonEndocytosisFluorescence Recovery After PhotobleachingGreen Fluorescent ProteinsProtein MultimerizationProtein StabilityRecombinant Fusion ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsTime-Lapse ImagingCytoskeletal ProteinsGreen Fluorescent ProteinsPil1 protein, S pombePil2 protein, S pombeRecombinant Fusion ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID21900489
PMCPMC3204068
OpenAlexW2057061786

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.