Evidence map›Paper›PMID 17182619›Full record

ArticleThe Journal of biological chemistry2007

Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein: implications for how capping protein binds the actin filament.

Kyoungtae Kim, Michelle E McCully, Nandini Bhattacharya, Boyd Butler, David Sept, John A Cooper

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

50 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Cardiac CapZ Regulation During Acute Exercise in Female Mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
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  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Review
  17. CAPZA1 modulates EMT by regulating actin cytoskeleton remodelling in hepatocellular carcinoma.Journal of experimental & clinical cancer research : CR · 2017
    Article
  18. Article
  19. Review
  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

6 authors at 1 institution in 1 country.

Kyoungtae KimDepartment of Cell Biology and Physiology.
Michelle E McCully
Nandini Bhattacharya
Boyd Butler
David Sept
John 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
DEVELOPMENTAL CARDIOLOGY AND PULMONARY TRAINING PROGRAMT32HL007873 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P. · 1998 to 2012
$3.6M
Protein interactions underlying actin-based motilityR01GM067246 · NIGMS · WASHINGTON UNIVERSITY · PI SEPT, DAVID S. · 2002 to 2006
$1.3M
NHLBI NIH HHS T32 HL007873NIGMS NIH HHS GM067246NIGMS NIH HHS GM38542NIGMS NIH HHS R01 GM038542NIGMS NIH HHS R01 GM067246
6 · The paper itself

Abstract

The heterodimeric actin-capping protein (CP) can be inhibited by polyphosphoinositides, which may be important for actin polymerization at membranes in cells. Here, we have identified a conserved set of basic residues on the surface of CP that are important for the interaction with phosphatidylinositol 4,5-bisphosphate (PIP(2)). Computational docking studies predicted the identity of residues involved in this interaction, and functional and physical assays with site-directed mutants of CP confirmed the prediction. The PIP(2) binding site overlaps with the more important of the two known actin-binding sites of CP. Correspondingly, we observed that loss of PIP(2) binding correlated with loss of actin binding among the mutants. Using TIRF (total internal reflection fluorescence) microscopy, we observed that PIP(2) rapidly converted capped actin filaments to a growing state, consistent with uncapping. Together, these results extend our understanding of how CP binds to the barbed end of the actin filament, and they support the idea that CP can "wobble" when bound to the barbed end solely by the C-terminal "tentacle" of its beta-subunit.

Indexed as

Models, MolecularActin Capping ProteinsActinsAnimalsBinding SitesHumansMutationPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein SubunitsRabbitsStructure-Activity RelationshipActin Capping ProteinsActinsPhosphatidylinositol 4,5-DiphosphateProtein Subunits

Identifiers

PMID17182619
PMCPMC2583367
OpenAlexW2022411637

What OpenQuestion holds

Textmetadata
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.