Evidence map›Paper›PMID 7896874›Full record

ArticleThe Journal of cell biology1995

Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin.

J Z Chuang, D C Lin, S Lin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-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

23 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. Tensin regulates pharyngeal pumping in Caenorhabditis elegans.Biochemical and biophysical research communications · 2020
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Small heat shock proteins in smooth muscle.Pharmacology & therapeutics · 2008
    Review
  11. Article
  12. Article
  13. Article
  14. Tensin1 and a previously undocumented family member, tensin2, positively regulate cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  15. Article
  16. Molecular characterization of human tensin.The Biochemical journal · 2000
    Article
  17. Article
  18. Article
  19. A 29 kDa intracellular chloride channel p64H1 is associated with large dense-core vesicles in rat hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  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

3 authors at 1 institution in 1 country.

J Z ChuangDepartment of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218-2684.
D C Lin
S Lin
Johns Hopkins University · US

Funding

CYTOCHALASINS, ACTIN FILAMENTS, AND CELL MOTILITYR01GM022289 · NIGMS · UNIVERSITY OF CALIFORNIA IRVINE · PI LIN, SHIN · 1985 to 1999
–
NIGMS NIH HHS GM22289
6 · The paper itself

Abstract

Tensin, an actin filament capping protein first purified from chicken gizzard, is localized to various types of adherens junctions in muscle and nonmuscle cells. In this paper, we describe the isolation and sequencing of tensin cDNA from a chicken cardiac library. The 6.3-kb chicken cardiac tensin cDNA encodes an open reading frame of 1,792 amino acids. Mammalian cells transfected with the chicken tensin cDNA expressed a polypeptide of approximately 200 kD recognizable by antibodies to chicken gizzard tensin. The expressed protein was incorporated into focal adhesions and other actin-containing structures in the transfected cells. To map the domain associated with tensin's high affinity, barbed-end F-actin-capping activity, bacterially expressed recombinant fusion proteins containing various segments of tensin were prepared and assayed for activity. The results of these experiments show that the high affinity capping domain (kD = 1.3 nM) lies within amino acid residues R1037-V1169. Additional studies on a shorter construct, S1061-H1145, showed that these 85 residues were sufficient for producing complete inhibition of actin polymerization and depolymerization. While this active domain is located within that of the "insertin" sequence (Weigt, C., A. Gaertner, A. Wegner, H. Korte, and H. E. Meyer. 1992. J. Mol. Biol. 227:593-595), our data showing complete inhibition of polymerization and shift in critical concentration are consistent with a simple barbed-end capping mechanism rather than the "insertin model." Our results also differ from those of a recent report (Lo, S. H., P. A. Janmey, J. H. Hartwig, and L. B. Chen. 1994. J. Cell Biol. 125:1067-1075), which concluded that their recombinant tensin has an "insertin-like" inhibitory effect on barbed-end actin polymerization, and that this activity is attributed to residues T936-R1037 (residues 888-989 in their numbering system). In our study, a fusion construct (N790-K1060) encompassing T936-R1037 had no significant effect on actin polymerization and depolymerization, even at high concentrations.

Indexed as

3T3 CellsActinsAmino Acid SequenceAnimalsBase SequenceCell LineChickensCloning, MolecularHumansMiceMicrofilament ProteinsMolecular Sequence DataMyocardiumProtein BindingRepetitive Sequences, Nucleic AcidSequence HomologyActinsMicrofilament ProteinsTensins

Identifiers

PMID7896874
PMCPMC2120419
OpenAlexW2077147160

What OpenQuestion holds

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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.