Evidence map›Paper›PMID 16450059›Full record

ArticleJournal of muscle research and cell motility2005

Dimerization of the cardiac ankyrin protein CARP: implications for MARP titin-based signaling.

Stephanie H Witt, Dietmar Labeit, Henk Granzier, Siegfried Labeit, Christian C Witt

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Article in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Review
  3. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Titin mutations and muscle disease.Pflugers Archiv : European journal of physiology · 2019
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 2017
    Review
  15. Article
  16. Review
  17. Review
  18. Desmin related disease: a matter of cell survival failure.Current opinion in cell biology · 2015
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Stephanie H WittInstitut für Anaesthesiologie und Operative Intensivmedizin, Universitätsklinikum Mannheim, 68167, Mannheim, Germany.
Dietmar Labeit
Henk Granzier
Siegfried Labeit
Christian C Witt

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cardiac ankyrin repeat protein (CARP) and its two close homologs ankrd2 (Arpp) and DARP correspond to a conserved gene family of muscle ankyrin repeat proteins (MARPs). All three genes respond to a variety of stress/strain injury signals with their cytokine-like induction and can associate with the elastic region of titin/connectin. Recently, both CARP and ankrd2 were observed to be elevated in cardiac diseases as well as muscular dystrophies, implicating their joined signaling in muscle diseases. Here we show that CARP in the yeast two-hybrid system (YTH) interacts with itself and desmin. To further verify the YTH data and to investigate possible CARP subunit structure(s), we expressed CARP in E. coli. Expressed CARP has an apparent mobility of about 70 kDa on gel filtration, corresponding to a dimeric species. Yeast two-hybrid experiments using amino- and carboxyterminal deletion clones suggest that CARP, ankrd2, and DARP contain potential coiled-coil dimerization motifs within their unique aminoterminal domains that mediate the formation of homo-dimers. In contrast, we could not detect the formation of hetero-dimers between CARP, ankrd2, and DARP. Therefore, when CARP, ankrd2 and DARP are upregulated in disease/stress states, they are likely to be sorted into distinct structural protein complexes since CARP within the MARP family contains a unique aminoterminal dimerization motif.

Indexed as

Signal TransductionAnkyrin RepeatConnectinDesminDimerizationEscherichia coliHumansMolecular WeightMuscle ProteinsNuclear ProteinsPeptide FragmentsProtein BindingProtein KinasesRecombinant ProteinsRepressor ProteinsTransfectionANKRD1 protein, humanANKRD23 protein, humanANKRD2 protein, humanConnectinDesminMuscle ProteinsNuclear ProteinsPeptide FragmentsProtein KinasesRecombinant ProteinsRepressor ProteinsTTN protein, human

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Registered trials

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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.