Evidence map›Paper›PMID 21416260›Full record

ReviewPflugers Archiv : European journal of physiology2011

Cytoskeletal protein kinases: titin and its relations in mechanosensing.

Mathias Gautel

Open access · hybridAbstract readReview
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

74 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. PK1 fromOpen biology · 2023
    Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Mechanisms of exercise as a preventative measure to muscle wasting.American journal of physiology. Cell physiology · 2021
    Review
  13. Review
  14. Exploring Obscurin and SPEG Kinase Biology.Journal of clinical medicine · 2021
    Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Unraveling obscurins in heart disease.Pflugers Archiv : European journal of physiology · 2019
    Review

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

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

1 author at 1 institution in 1 country.

Mathias GautelKing's College London BHF Centre of Research Excellence, Cardiovascular Division, London, SE1 1UL, UK. mathias.gautel@kcl.ac.uk
King's College London · GB

Funding

British Heart FoundationMedical Research Council G0200496Medical Research Council G0600251Wellcome Trust
6 · The paper itself

Abstract

Titin, the giant elastic ruler protein of striated muscle sarcomeres, contains a catalytic kinase domain related to a family of intrasterically regulated protein kinases. The most extensively studied member of this branch of the human kinome is the Ca(2+)-calmodulin (CaM)-regulated myosin light-chain kinases (MLCK). However, not all kinases of the MLCK branch are functional MLCKs, and about half lack a CaM binding site in their C-terminal autoinhibitory tail (AI). A unifying feature is their association with the cytoskeleton, mostly via actin and myosin filaments. Titin kinase, similar to its invertebrate analogue twitchin kinase and likely other "MLCKs", is not Ca(2+)-calmodulin-activated. Recently, local protein unfolding of the C-terminal AI has emerged as a common mechanism in the activation of CaM kinases. Single-molecule data suggested that opening of the TK active site could also be achieved by mechanical unfolding of the AI. Mechanical modulation of catalytic activity might thus allow cytoskeletal signalling proteins to act as mechanosensors, creating feedback mechanisms between cytoskeletal tension and tension generation or cellular remodelling. Similar to other MLCK-like kinases like DRAK2 and DAPK1, TK is linked to protein turnover regulation via the autophagy/lysosomal system, suggesting the MLCK-like kinases have common functions beyond contraction regulation.

Indexed as

Amino Acid SequenceAnimalsConnectinCytoskeletal ProteinsCytoskeletonHumansMechanotransduction, CellularModels, MolecularMolecular Sequence DataMuscle ProteinsMyosin-Light-Chain KinasePhylogenyProtein ConformationProtein FoldingProtein KinasesProtein UnfoldingConnectinCytoskeletal ProteinsMuscle ProteinsMyosin-Light-Chain KinaseProtein KinasesTTN protein, human

Identifiers

PMID21416260
PMCPMC3114093
OpenAlexW2028687363

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.