Evidence map›Paper›PMID 19278997›Full record

ArticleThe Journal of biological chemistry2009

Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions.

Mirko Himmel, Anett Ritter, Sven Rothemund, Björg V Pauling, Klemens Rottner, Alexandre R Gingras, Wolfgang H Ziegler

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Hemidesmosome-Related Keratin Filament Bundling and Nucleation.International journal of molecular sciences · 2021
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Selective Role of Vinculin in Contractile Mechanisms of Endothelial Permeability.American journal of respiratory cell and molecular biology · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

7 authors.

Mirko HimmelInterdisciplinary Centre for Clinical Research (IZKF) Leipzig, Faculty of Medicine, University of Leipzig, D-04103 Leipzig, Germany.
Anett RitterInterdisciplinary Centre for Clinical Research (IZKF) Leipzig, Faculty of Medicine, University of Leipzig, D-04103 Leipzig, Germany.
Sven RothemundInterdisciplinary Centre for Clinical Research (IZKF) Leipzig, Faculty of Medicine, University of Leipzig, D-04103 Leipzig, Germany.
Björg V PaulingZoological Institute, Technical University of Braunschweig, D-38106 Braunschweig, Germany.
Klemens RottnerCytoskeleton Dynamics Group, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.
Alexandre R GingrasDepartment of Biochemistry, University of Leicester, Leicester LE1 9HN, United Kingdom.
Wolfgang H ZieglerInterdisciplinary Centre for Clinical Research (IZKF) Leipzig, Faculty of Medicine, University of Leipzig, D-04103 Leipzig, Germany. Electronic address: wolfgang.ziegler@medizin.uni-leipzig.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In cell-extracellular matrix junctions (focal adhesions), the cytoskeletal protein talin is central to the connection of integrins to the actin cytoskeleton. Talin is thought to mediate this connection via its two integrin, (at least) three actin, and several vinculin binding sites. The binding sites are cryptic in the head-to-rod autoinhibited cytoplasmic form of the protein and require (stepwise) conformational activation. This activation process, however, remains poorly understood, and there are contradictory models with respect to the determinants of adhesion site localization. Here, we report turnover rates and protein-protein interactions in a range of talin rod domain constructs varying in helix bundle structure. We conclude that several bundles of the C terminus cooperate to regulate targeting and concomitantly tailor high affinity interactions of the talin rod in cell adhesions. Intrinsic control of ligand binding activities is essential for the coordination of adhesion site function of talin.

Indexed as

Models, BiologicalActinsAnimalsBinding SitesCell AdhesionCell LineCytoskeletonFocal AdhesionsIntegrinsMiceProtein Structure, SecondaryProtein Structure, TertiaryTalinActinsIntegrinsTalinTln1 protein, mouse

Identifiers

PMID19278997
PMCPMC2679484

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.