Evidence map›Paper›PMID 8858171›Full record

ArticleThe Journal of cell biology1996

Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.

D A Schafer, P B Jennings, J A Cooper

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 187 papers.

0numbers the graph read from it
0cells of the map it votes in
187citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

187 citing papers in PubMed, 419 citations in OpenAlex.

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  18. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  19. Article
  20. Article

127 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

D A SchaferDepartment of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri 63110, USA. dorothy@cellbio.wustl.edu
P B Jennings
J A Cooper
Washington University in St. Louis · US

Funding

Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
NIGMS NIH HHS GM 38542NIGMS NIH HHS R01 GM038542
6 · The paper itself

Abstract

Bursts of actin polymerization in vivo involve the transient appearance of free barbed ends. To determine how rapidly barbed ends might appear and how long they might remain free in vivo, we studied the kinetics of capping protein, the major barbed end capper, binding to barbed ends in vitro. First, the off-rate constant for capping protein leaving a barbed end is slow, predicting a half-life for a capped barbed end of approximately 30 min. This half-life implies that cells cannot wait for capping protein to spontaneously dissociate from capped barbed ends in order to create free barbed ends. However, we find that phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 4-mono-phosphate (PIP) cause rapid and efficient dissociation of capping protein from capped filaments. PIP2 is a strong candidate for a second messenger regulating actin polymerization; therefore, the ability of PIP2 to remove capping protein from barbed ends is a potential mechanism for stimulating actin polymerization in vivo. Second, the on-rate constant for capping protein binding to free barbed ends predicts that actin filaments could grow to the length of filaments observed in vivo during one lifetime. Third, capping protein beta-subunit isoforms did not differ in their actin binding properties, even in tests with different actin isoforms. A major hypothesis for why capping protein beta-subunit isoforms exist is thereby excluded. Fourth, the proposed capping protein regulators, Hsc70 and S100, had no effect on capping protein binding to actin in vitro.

Indexed as

HSP70 Heat-Shock ProteinsActin Depolymerizing FactorsActinsAnimalsBrain ChemistryCapZ Actin Capping ProteinCarrier ProteinsChickensDestrinErythrocytesHSC70 Heat-Shock ProteinsKidneyKineticsMicrofilament ProteinsMuscle ProteinsMuscle, SkeletalActin Depolymerizing FactorsActinsCapZ Actin Capping ProteinCarrier ProteinsDestrinHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMicrofilament ProteinsMuscle ProteinsPhosphatidylinositol PhosphatesS100 Proteins

Identifiers

PMID8858171
PMCPMC2121029
OpenAlexW2157151771

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.