Evidence map›Paper›PMID 1661732›Full record

ArticleThe Journal of cell biology1991

Direct observation of actin filament severing by gelsolin and binding by gCap39 and CapZ.

E L Bearer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-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

26 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. New insights into mechanism and regulation of actin capping protein.International review of cell and molecular biology · 2008
    Review
  9. Article
  10. Article
  11. Actin dynamics in platelets.International review of cytology · 2002
    Review
  12. Article
  13. Article
  14. Calcium influx alters actin bundle dynamics and retrograde flow in Helisoma growth cones.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  15. Article
  16. Article
  17. An axoplasmic myosin with a calmodulin-like light chain.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  18. Actin-based motility of isolated axoplasmic organelles.Cell motility and the cytoskeleton · 1996
    Article
  19. Review
  20. Cytoskeletal domains in the activated platelet.Cell motility and the cytoskeleton · 1995
    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

1 author at 1 institution in 1 country.

E L BearerDivision of Biology and Medicine, Brown University, Providence, Rhode Island. 02912.
Brown University · US

Funding

GENETIC AND BIOCHEMICAL ANALYSIS OF CYTOKINESISR01GM023928 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1985 to 2010
$3.6M
NIGMS NIH HHS GM 23928
6 · The paper itself

Abstract

Dynamic behavior of actin filaments in cells is the basis of many different cellular activities. Remodeling of the actin filament network involves polymerization and depolymerization of the filaments. Proteins that regulate these behaviors include proteins that sever and/or cap actin filaments. This report presents direct observation of severing of fluorescently-labeled actin filaments. Coverslips coated with gelsolin, a multi-domain, calcium-dependent capping and severing protein, bound rhodamine-phalloidin-saturated filaments along their length in the presence of EGTA. Upon addition of calcium, attached filaments bent as they broke. Actophorin, a low molecular weight, monomer sequestering, calcium-independent severing protein did not sever phalloidin-saturated filaments. Both gCap 39, a gelsolin-like, calcium-dependent capping protein that does not sever filaments, and CapZ, a heterodimeric, non-calcium-dependent capping protein, bound the filaments by one end to the coverslip. Visualization of individual filaments also revealed severing activity present in mixtures of actin-binding proteins isolated by filamentous actin affinity chromatography from early Drosophila embryos. This activity was different from either gelsolin or actophorin because it was not inhibited by phalloidin, but was calcium independent. The results of these studies provide new information about the molecular mechanisms of severing and capping by well-characterized proteins as well as definition of a novel type of severing activity.

Indexed as

Nuclear ProteinsActinsAdenosine TriphosphateAnimalsCalciumCalcium-Binding ProteinsCapZ Actin Capping ProteinChromatography, AffinityDrosophilaElectrophoresis, Polyacrylamide GelGelsolinMicrofilament ProteinsMuscle ProteinsPhalloidineProtein BindingRabbitsActinsAdenosine TriphosphateCalciumCalcium-Binding ProteinsCapZ Actin Capping ProteinGelsolinMicrofilament ProteinsMuscle ProteinsNuclear ProteinsPhalloidine

Identifiers

PMID1661732
PMCPMC2289206
OpenAlexW1986214836

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.