Evidence map›Paper›PMID 8294516›Full record

ArticleThe Journal of cell biology1994

The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity.

R A Van Etten, P K Jackson, D Baltimore, M C Sanders, P T Matsudaira, P A Janmey

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

107 citing papers in PubMed, 270 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Tyrosine kinase inhibitors and interferon-α increase tunneling nanotube (TNT) formation and cell adhesion in chronic myeloid leukemia (CML) cell lines.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Global Regulation of Differential Gene Expression by c-Abl/Arg Oncogenic Kinases.Medical science monitor : international medical journal of experimental and clinical research · 2017
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

R A Van EttenDepartment of Genetics, Harvard Medical School, Boston, Massachusetts 02115.
P K Jackson
D Baltimore
M C Sanders
P T Matsudaira
P A Janmey
Harvard University · US

Funding

REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR01AR038910 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI JANMEY, PAUL A · 1991 to 2006
$2.2M
MALIGNANCY AND NORMAL DEVELOPMENT IN PREB LYMPHOCYTESR01CA051462 · NCI · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BALTIMORE, DAVID · 1990 to 2004
$1.9M
STRUCTURE AND FUNCTION OF THE INTESTINE BRUSH BORDERR01DK035306 · NIDDK · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI MATSUDAIRA, PAUL T. · 1986 to 1992
–
REVERSIBLE FORMATION AND STRUCTURE OF ACTIN NETWORKSR29AR038910 · NIAMS · MASSACHUSETTS GENERAL HOSPITAL · PI JANMEY, PAUL A · 1987 to 1989
–
NCI NIH HHS CA51462NIAMS NIH HHS AR38910NIDDK NIH HHS DK35306
6 · The paper itself

Abstract

The myristoylated form of c-Abl protein, as well as the P210bcr/abl protein, have been shown by indirect immunofluorescence to associate with F-actin stress fibers in fibroblasts. Analysis of deletion mutants of c-Abl stably expressed in fibroblasts maps the domain responsible for this interaction to the extreme COOH-terminus of Abl. This domain mediates the association of a heterologous protein with F-actin filaments after microinjection into NIH 3T3 cells, and directly binds to F-actin in a cosedimentation assay. Microinjection and cosedimentation assays localize the actin-binding domain to a 58 amino acid region, including a charged motif at the extreme COOH-terminus that is important for efficient binding. F-actin binding by Abl is calcium independent, and Abl competes with gelsolin for binding to F-actin. In addition to the F-actin binding domain, the COOH-terminus of Abl contains a proline-rich region that mediates binding and sequestration of G-actin, and the Abl F- and G-actin binding domains cooperate to bundle F-actin filaments in vitro. The COOH terminus of Abl thus confers several novel localizing functions upon the protein, including actin binding, nuclear localization, and DNA binding. Abl may modify and receive signals from the F-actin cytoskeleton in vivo, and is an ideal candidate to mediate signal transduction from the cell surface and cytoskeleton to the nucleus.

Indexed as

3T3 CellsActin CytoskeletonActinsAnimalsBinding, CompetitiveBinding SitesFluorescent Antibody TechniqueGelsolinMiceMicroinjectionsProto-Oncogene Proteins c-ablRecombinant Fusion ProteinsActinsGelsolinProto-Oncogene Proteins c-ablRecombinant Fusion Proteins

Identifiers

PMID8294516
PMCPMC2119935
OpenAlexW2162245996

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.