ArticleLife science alliance2019
An extracellular matrix protein promotes anillin-dependent processes in the
Article in Life science alliance, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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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.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- EmbSAM: cell boundary localization and Segment Anything Model for fast images of developing embryos.Communications biology · 2025Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.Molecular biology of the cell · 2025Article
- Characterization of Maturation-Associated Genes in Ovary-Hepatopancreas Transcriptome andAnimals : an open access journal from MDPI · 2025Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.bioRxiv : the preprint server for biology · 2025Article
- A nucleic acid binding protein map of germline regulation in Caenorhabditis elegans.Nature communications · 2024Article
- Cortical recruitment of centralspindlin and RhoA effectors during meiosis I ofJournal of cell science · 2021Article
- Chondroitin sulfate in invertebrate development.Proteoglycan researchArticle
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell division requires constriction of an actomyosin ring to segregate the genetic material equally into two daughter cells. The spatial and temporal regulation of the contractile ring at the division plane primarily depends on intracellular signals mediated by the centralspindlin complex and astral microtubules. Although much investigative work has elucidated intracellular factors and mechanisms controlling this process, the extracellular regulation of cytokinesis remains unclear. Thus far, the extracellular matrix protein Hemicentin (HIM-4) has been proposed to be required for cleavage furrow stabilization. The underlying molecular mechanism, however, has remained largely unknown. Here, we show that HIM-4 and anillin (ANI-1) genetically act in the same pathway to maintain the rachis bridge stability in the germline. Our FRAP experiments further reveal that HIM-4 restricts the motility of ANI-1. In addition, we demonstrate that HIM-4 is recruited to the cleavage site in dividing germ cells and promotes the proper ingression of the cleavage membrane. Collectively, we propose that HIM-4 is an extracellular factor that regulates ANI-1 for germ cell membrane stabilization and contractile ring formation in
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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.