ArticleProceedings of the National Academy of Sciences of the United States of America2012
Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed.
- STRIPAK-associated greenbeard proteins DOC1 and DOC2 regulate MAK2 signaling and sexual development in Sordaria macrospora.PLoS biology · 2026Article
- Low-complexity regions in fungi display functional groups and are depleted in positively charged amino acids.NAR genomics and bioinformatics · 2025Article
- The clock in growing hyphae and their synchronization in Neurospora crassa.Communications biology · 2024Article
- Cytoplasmic zoning by protein phase transition after membrane permeabilization.Journal of biochemistry · 2024Review
- Article
- Article
- Pathogen-specific structural features ofmBio · 2023Article
- Woronin body hitchhiking on early endosomes is dispensable for septal localization inMolecular biology of the cell · 2023Article
- Large-scale identification of genes involved in septal pore plugging in multicellular fungi.Nature communications · 2023Article
- Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions.Biomolecules · 2021Article
- Hex1, the Major Component of Woronin Bodies, Is Required for Normal Development, Pathogenicity, and Stress Response in the Plant Pathogenic FungusJournal of fungi (Basel, Switzerland) · 2020Article
- Syncytia in Fungi.Cells · 2020Review
- Arginine-Enriched Mixed-Charge Domains Provide Cohesion for Nuclear Speckle Condensation.Molecular cell · 2020Article
- Conserved Eukaryotic Kinase CK2 Chaperone Intrinsically Disordered Protein Interactions.Applied and environmental microbiology · 2020Article
- VelA and LaeA are Key Regulators ofMicroorganisms · 2019Article
- The Significance of the Intrinsically Disordered Regions for the Functions of the bHLH Transcription Factors.International journal of molecular sciences · 2019Review
- Article
- Fungal Morphogenesis, from the Polarized Growth of Hyphae to Complex Reproduction and Infection Structures.Microbiology and molecular biology reviews : MMBR · 2018Review
- Woronin body-based sealing of septal pores.Fungal genetics and biology : FG & B · 2017Article
- ATP prevents Woronin bodies from sealing septal pores in unwounded cells of the fungus Zymoseptoria tritici.Cellular microbiology · 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
9 authors.
Funding
Abstract
Like animals and plants, multicellular fungi possess cell-to-cell channels (septal pores) that allow intercellular communication and transport. Here, using a combination of MS of Woronin body-associated proteins and a bioinformatics approach that identifies related proteins based on composition and character, we identify 17 septal pore-associated (SPA) proteins that localize to the septal pore in rings and pore-centered foci. SPA proteins are not homologous at the primary sequence level but share overall physical properties with intrinsically disordered proteins. Some SPA proteins form aggregates at the septal pore, and in vitro assembly assays suggest aggregation through a nonamyloidal mechanism involving mainly α-helical and disordered structures. SPA loss-of-function phenotypes include excessive septation, septal pore degeneration, and uncontrolled Woronin body activation. Together, our data identify the septal pore as a complex subcellular compartment and focal point for the assembly of unstructured proteins controlling diverse aspects of intercellular connectivity.
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.