Evidence map›Paper›PMID 10548541›Full record

ArticleThe Biochemical journal1999

Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins.

B D Leinweber, P C Leavis, Z Grabarek, C L Wang, K G Morgan

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 134 citations in OpenAlex.

  1. Review
  2. Evolution and function of calponin and transgelin.Frontiers in cell and developmental biology · 2023
    Review
  3. Article
  4. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  5. Review
  6. Structure and Emerging Functions of LRCH Proteins in Leukocyte Biology.Frontiers in cell and developmental biology · 2020
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Role of SM22 in the differential regulation of phasic vs. tonic smooth muscle.American journal of physiology. Gastrointestinal and liver physiology · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. Hierarchical scaffolding of an ERK1/2 activation pathway.Cell communication and signaling : CCS · 2013
    Article
  20. Review
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

5 authors at 2 institutions in 1 country.

B D LeinweberBoston Biomedical Research Institute, 20 Staniford Street, Boston, MA 02114-2500, USA.
P C Leavis
Z Grabarek
C L Wang
K G Morgan
Boston Biomedical Research Institute · USTufts University · US

Funding

REGULATION OF CONTRACTION OF BLOOD VESSELSR01HL031704 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 1985 to 2009
$3.7M
CONTRACTION OF VASCULAR SMOOTH MUSCLE CELLSR01HL042293 · NHLBI · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI MORGAN, KATHLEEN G · 1989 to 2004
$1.2M
NHLBI NIH HHS HL10026NHLBI NIH HHS HL31704NHLBI NIH HHS HL42293
6 · The paper itself

Abstract

An interaction between extracellular regulated kinase 1 (ERK1) and calponin has previously been reported (Menice, Hulvershorn, Adam, Wang and Morgan (1997) J. Biol. Chem. 272 (40), 25157-25161) and has been suggested to reflect a function of calponin as a signalling molecule. We report in this study that calponin binds to both ERK1 and ERK2 under native conditions as well as in an overlay assay. Using chymotryptic fragments of calponin, the binding site of ERK on calponin was identified as the calponin homology (CH) domain, an N-terminal region of calponin found in other actin-binding proteins. ERK also bound, in a gel overlay assay, alpha-actinin, a protein with two tandem CH domains, as well as a 27 kDa thermolysin product of alpha-actinin containing the CH domains of alpha-actinin. The CH domain of calponin could compete with intact calponin or alpha-actinin for ERK binding. Titration of acrylodan-labelled calponin with ERK gave a K(a) of 6x10(6) M(-1) and titration of acrylodan-labelled calponin with a peptide from the alphaL16 helix of ERK gave a K(a) of 1x10(6) M(-1). Recombinant ERK was found to co-sediment with purified actin and induced a fluorescence change in pyrene-labelled F-actin (K(a)=5x10(6) M(-1)). The interaction of ERK with CH domains points to a new potential function for CH domains. The interaction of ERK with actin raises the possibility that actin may provide a scaffold for ERK signalling complexes in both muscle and non-muscle cells.

Indexed as

ActininActinsAnimalsBinding, CompetitiveBinding SitesCalcium-Binding ProteinsCalponinsIn Vitro TechniquesKineticsMicrofilament ProteinsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPeptide FragmentsProtein BindingProtein Structure, TertiaryActininActinsCalcium-Binding ProteinsCalponinsMicrofilament ProteinsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPeptide Fragments

Identifiers

PMID10548541
PMCPMC1220621
OpenAlexW2040508577

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.