Evidence map›Paper›PMID 10477759›Full record

ArticleThe Journal of cell biology1999

Filamin is required for ring canal assembly and actin organization during Drosophila oogenesis.

M G Li, M Serr, K Edwards, S Ludmann, D Yamamoto, L G Tilney, C M Field, T S Hays

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. 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
2.1field-weighted citation impact, top 13% 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, 83 citations in OpenAlex.

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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

8 authors at 5 institutions in 2 countries.

M G LiDepartment of Genetics, Cell and Developmental Biology, University of Minnesota, St. Paul, Minnesota 55108, USA.
M Serr
K Edwards
S Ludmann
D Yamamoto
L G Tilney
C M Field
T S Hays
University of Minnesota · USHarvard University · USUniversity of Hawaii System · USUniversity of Pennsylvania · USWaseda University · JP

Funding

GENETIC AND BIOCHEMICAL ANALYSIS OF CYTOKINESISR01GM023928 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1985 to 2010
$3.6M
PATTERN GENERATION OF ACTIN FILAMENTSR37GM052857 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI TILNEY, LEWIS G · 1995 to 2004
$1.6M
CELL POLARITY AND CYTOSKELETAL TRANSPORT IN DROSOPHILAR01GM053695 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HAYS, THOMAS S · 1996 to 2006
$1.1M
GENETIC ANALYSES OF CYTOPLASMIC DYNEIN IN DROSOPHILAF32GM017485 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI LI, MIN-GANG · 1995 to 1996
–
NIGMS NIH HHS F32 GM017485NIGMS NIH HHS GM 17485NIGMS NIH HHS GM23928NIGMS NIH HHS GM52857NIGMS NIH HHS R01 GM023928NIGMS NIH HHS R01 GM053695NIGMS NIH HHS R37 GM052857
6 · The paper itself

Abstract

The remodeling of the actin cytoskeleton is essential for cell migration, cell division, and cell morphogenesis. Actin-binding proteins play a pivotal role in reorganizing the actin cytoskeleton in response to signals exchanged between cells. In consequence, actin-binding proteins are increasingly a focus of investigations into effectors of cell signaling and the coordination of cellular behaviors within developmental processes. One of the first actin-binding proteins identified was filamin, or actin-binding protein 280 (ABP280). Filamin is required for cell migration (Cunningham et al. 1992), and mutations in human alpha-filamin (FLN1; Fox et al. 1998) are responsible for impaired migration of cerebral neurons and give rise to periventricular heterotopia, a disorder that leads to epilepsy and vascular disorders, as well as embryonic lethality. We report the identification and characterization of a mutation in Drosophila filamin, the homologue of human alpha-filamin. During oogenesis, filamin is concentrated in the ring canal structures that fortify arrested cleavage furrows and establish cytoplasmic bridges between cells of the germline. The major structural features common to other filamins are conserved in Drosophila filamin. Mutations in Drosophila filamin disrupt actin filament organization and compromise membrane integrity during oocyte development, resulting in female sterility. The genetic and molecular characterization of Drosophila filamin provides the first genetic model system for the analysis of filamin function and regulation during development.

Indexed as

ActinsAmino Acid SequenceAnimalsBiological TransportCell AdhesionCell MembraneCell SizeCloning, MolecularContractile ProteinsCytoplasmDrosophila melanogasterFemaleFertilityFilaminsGenes, InsectHumansActinsContractile ProteinsFilaminsFLNA protein, humanFLNC protein, humanMicrofilament ProteinsPeptides

Identifiers

PMID10477759
PMCPMC2169474
OpenAlexW2115410831

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.