Evidence map›Paper›PMID 20707996›Full record

ArticleDevelopmental biology2010

FLN-1/filamin is required for maintenance of actin and exit of fertilized oocytes from the spermatheca in C. elegans.

Ismar Kovacevic, Erin J Cram

Open access · greenAbstract read
In one paragraph

Article in Developmental biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

35 citing papers in PubMed, 57 citations in OpenAlex.

  1. PES-8 is required for Cytoskeletal Organization and Contractility in thebioRxiv : the preprint server for biology · 2026
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  6. Tensions on the actin cytoskeleton and apical cell junctions in thebioRxiv : the preprint server for biology · 2024
    Article
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  9. Tensions on the actin cytoskeleton and apical cell junctions in theFrontiers in cell and developmental biology · 2024
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  18. Regulation of Actin Dynamics in theJournal of developmental biology · 2019
    Review
  19. TheDevelopment (Cambridge, England) · 2019
    Article
  20. Article
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

2 authors at 1 institution in 1 country.

Ismar KovacevicDepartment of Biology, Northeastern University, 134 Mugar Hall, 360 Huntington Ave, Boston, MA 02115, USA.
Erin J Cram
Northeastern University · US

Funding

Characterization of a novel regulator of cell migrationR01GM085077 · NIGMS · NORTHEASTERN UNIVERSITY · PI CRAM, ERIN JEAN · 2008 to 2012
$1.4M
NIGMS NIH HHS R01 GM085077
6 · The paper itself

Abstract

Filamin, known primarily for its actin cross-linking function, is a stretch-sensitive structural and signaling scaffold that binds transmembrane receptors and a wide variety of intracellular signaling proteins. The Caenorhabditis elegans filamin ortholog, FLN-1, has a well conserved overall structure, including an N-terminal actin-binding domain, and a series of 20 immunoglobulin (Ig)-like repeats. FLN-1 partially colocalizes with actin filaments in spermathecal and uterine cells. Analysis of phenotypes resulting from a deletion allele and RNAi depletion indicates FLN-1 is required to maintain the actin cytoskeleton in the spermatheca and uterus, and to allow the exit of embryos from the spermatheca. FLN-1 deficient animals accumulate embryos in the spermatheca, lay damaged and unfertilized eggs, and consequently exhibit dramatically reduced brood sizes. The phospholipase PLC-1 is also required for the exit of embryos from the spermatheca, and analysis of doubly mutant animals suggests that PLC-1 and FLN-1 act in the same pathway to promote proper transit of embryos from the spermatheca to the uterus. Given the modular protein structure, subcellular localization, genetic interaction with PLC-1, and known mechanosensory functions of filamin, we postulate that FLN-1 may be required to convert mechanical information about the presence of the oocyte into a biochemical signal, thereby allowing timely exit of the embryo from the spermatheca.

Indexed as

ActinsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsContractile ProteinsFemaleFertilityFilaminsGenitaliaMaleMicrofilament ProteinsOocytesProtein IsoformsRNA InterferenceSignal TransductionActinsCaenorhabditis elegans ProteinsContractile ProteinsFilaminsFLN-1 protein, C elegansMicrofilament ProteinsProtein Isoforms

Identifiers

PMID20707996
PMCPMC2957521
OpenAlexW1986279095

What OpenQuestion holds

Textmetadata
LicenceTDM
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.