ArticleMolecular biology of the cell2006
Ppc89 links multiple proteins, including the septation initiation network, to the core of the fission yeast spindle-pole body.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
Who cites it
33 citing papers in PubMed, 59 citations in OpenAlex.
- New mutations in the core Schizosaccharomyces pombe spindle pole body scaffold Ppc89 reveal separable functions in regulating cell division.G3 (Bethesda, Md.) · 2025Article
- The core spindle pole body scaffold Ppc89 links the pericentrin orthologue Pcp1 to the fission yeast spindle pole body via an evolutionarily conserved interface.Molecular biology of the cell · 2024Article
- Transient PP2A SIP complex localization to mitotic SPBs for SIN inhibition is mediated solely by the Csc1 FHA domain.Molecular biology of the cell · 2024Article
- A role for the carbon source of the cell and protein kinase A in regulating the S. pombe septation initiation network.Journal of cell science · 2024Article
- An ESCRT grommet cooperates with a diffusion barrier to maintain nuclear integrity.Nature cell biology · 2023Article
- Review
- The N-terminus of Sfi1 and yeast centrin Cdc31 provide the assembly site for a new spindle pole body.The Journal of cell biology · 2021Article
- Anatomy of the fungal microtubule organizing center, the spindle pole body.Current opinion in structural biology · 2021Review
- Tell the Difference Between Mitosis and Meiosis: Interplay Between Chromosomes, Cytoskeleton, and Cell Cycle Regulation.Frontiers in cell and developmental biology · 2021Review
- TheJournal of cell science · 2019Article
- Article
- Structure and function of Spc42 coiled-coils in yeast centrosome assembly and duplication.Molecular biology of the cell · 2019Article
- The Cep57-pericentrin module organizes PCM expansion and centriole engagement.Nature communications · 2019Article
- Relief of the Dma1-mediated checkpoint requires Dma1 autoubiquitination and dynamic localization.Molecular biology of the cell · 2018Article
- Involvement of the septation initiation network in events during cytokinesis in fission yeast.Journal of cell science · 2018Article
- Centrosome Remodelling in Evolution.Cells · 2018Review
- The kinase domain of CK1 enzymes contains the localization cue essential for compartmentalized signaling at the spindle pole.Molecular biology of the cell · 2018Article
- Review
- Dialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment.The Journal of cell biology · 2017Article
- Molecular model of fission yeast centrosome assembly determined by superresolution imaging.The Journal of cell biology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
The spindle-pole body (SPB), the yeast analog of the centrosome, serves as the major microtubule (MT) organizing center in the yeast cell. In addition to this central function, the SPB organizes and concentrates proteins required for proper coordination between the nuclear-division cycle and cytokinesis. For example, the Schizosaccharomyces pombe septation-initiation network (SIN), which is responsible for initiating actomyosin ring constriction and septation, is assembled at the SPB through its two scaffolding components, Sid4 and Cdc11. In an effort to identify novel SIN interactors, we purified Cdc11 and identified by mass spectrometry a previously uncharacterized protein associated with it, Ppc89. Ppc89 localizes constitutively to the SPB and interacts directly with Sid4. A fusion between the N-terminal 300 amino acids of Sid4 and a SPB targeting domain of Ppc89 supplies the essential function of Sid4 in anchoring the SIN. ppc89Delta cells are inviable and exhibit defects in SPB integrity, and hence in spindle formation, chromosome segregation, and SIN localization. Ppc89 overproduction is lethal, resulting primarily in a G2 arrest accompanied by massive enlargement of the SPB and increased SPB MT nucleation. These results suggest a fundamental role for Ppc89 in organization of the S. pombe SPB.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.