Evidence map›Paper›PMID 10330414›Full record

ArticleThe Journal of cell biology1999

A molecular mechanism of integrin crosstalk: alphavbeta3 suppression of calcium/calmodulin-dependent protein kinase II regulates alpha5beta1 function.

S D Blystone, S E Slater, M P Williams, M T Crow, E J Brown

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Information processing during phagocytosis.Nature reviews. Immunology · 2012
    Review
  12. Article
  13. Molecular architecture and function of matrix adhesions.Cold Spring Harbor perspectives in biology · 2011
    Review
  14. Article
  15. Review
  16. Review
  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

5 authors at 4 institutions in 1 country.

S D BlystoneDepartment of Anatomy and Cell Biology, State University of New York, Health Science Center at Syracuse, Syracuse, New York 13210, USA. blystons@vax.cs.hscsyr.edu
S E Slater
M P Williams
M T Crow
E J Brown
National Institutes of Health · USNational Institute on Aging · USUniversity of California, San Francisco · USWashington University in St. Louis · US

Funding

EXTRACELLULAR MATRIX PROTEIN ENHANCEMENT OF PHAGOCYTOSISR01GM038330 · NIGMS · WASHINGTON UNIVERSITY · PI VONZASTROW, MARK E · 1987 to 2007
$2.7M
NOVEL LYMPHOCYTE INTEGRINSR01AI024674 · NIAID · WASHINGTON UNIVERSITY · PI SHEPPARD, DEAN · 1988 to 2009
$1.7M
NOVEL LEUKOCYTE INTEGRINSR37AI024674 · NIAID · WASHINGTON UNIVERSITY · PI BROWN, ERIC J. · 1996 to 2004
$1.4M
SIGNAL TRANSDUCTION PATHWAYS INVOLVED IN VASCULAR SMOOTH MUSCLE CELL MIGRATIONZ01AG000815 · NIA · AGING · PI CROW, MICHAEL T. · 1993 to 2001
–
NIAID NIH HHS AI08990-02NIAID NIH HHS AI24674NIAID NIH HHS R01 AI024674NIAID NIH HHS R37 AI024674NIGMS NIH HHS GM38330NIGMS NIH HHS R01 GM038330
6 · The paper itself

Abstract

Many cells express more than one integrin receptor for extracellular matrix, and in vivo these receptors may be simultaneously engaged. Ligation of one integrin may influence the behavior of others on the cell, a phenomenon we have called integrin crosstalk. Ligation of the integrin alphavbeta3 inhibits both phagocytosis and migration mediated by alpha5beta1 on the same cell, and the beta3 cytoplasmic tail is necessary and sufficient for this regulation of alpha5beta1. Ligation of alpha5beta1 activates the calcium- and calmodulin-dependent protein kinase II (CamKII). This activation is required for alpha5beta1-mediated phagocytosis and migration. Simultaneous ligation of alphavbeta3 or expression of a chimeric molecule with a free beta3 cytoplasmic tail prevents alpha5beta1-mediated activation of CamKII. Expression of a constitutively active CamKII restores alpha5beta1 functions blocked by alphavbeta3-initiated integrin crosstalk. Thus, alphavbeta3 inhibition of alpha5beta1 activation of CamKII is required for its role in integrin crosstalk. Structure-function analysis of the beta3 cytoplasmic tail demonstrates a requirement for Ser752 in beta3-mediated suppression of CamKII activation, while crosstalk is independent of Tyr747 and Tyr759, implicating Ser752, but not beta3 tyrosine phosphorylation in initiation of the alphavbeta3 signal for integrin crosstalk.

Indexed as

Calcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Cell MovementCells, CulturedHumansK562 CellsMacrophagesReceptors, FibronectinReceptors, VitronectinSerineCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Receptors, FibronectinReceptors, VitronectinSerine

Identifiers

PMID10330414
PMCPMC2133176
OpenAlexW1919621005

What OpenQuestion holds

Textmetadata
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.