Evidence map›Paper›PMID 18613116›Full record

ArticleCell motility and the cytoskeleton2008

CaMK-II promotes focal adhesion turnover and cell motility by inducing tyrosine dephosphorylation of FAK and paxillin.

Charles A Easley, Claire M Brown, Alan F Horwitz, Robert M Tombes

Open access · greenAbstract read
In one paragraph

Article in Cell motility and the cytoskeleton, 2008. 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
2.4field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Intracellular signaling dynamics and their role in coordinating tissue repair.Wiley interdisciplinary reviews. Systems biology and medicine · 2020
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Mitochondrial CaScientific reports · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Cellular control of connective tissue matrix tension.Journal of cellular biochemistry · 2013
    Review
  17. Article
  18. CaMKIIβ regulates oligodendrocyte maturation and CNS myelination.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  19. 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

4 authors at 2 institutions in 2 countries.

Charles A EasleyDepartment of Biochemistry and Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, USA.
Claire M Brown
Alan F Horwitz
Robert M Tombes
University of Virginia · USVirginia Commonwealth University · US

Funding

DETERMINANTS OF MYOGENIC MEMBRANE PHENOMENAR37GM023244 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HORWITZ, ALAN F · 1992 to 2002
$1.1M
NIGMS NIH HHS R37 GM023244
6 · The paper itself

Abstract

Transient elevations in Ca2+ have previously been shown to promote focal adhesion disassembly and cell motility through an unknown mechanism. In this study, evidence is provided to show that CaMK-II, a Ca2+/calmodulin dependent protein kinase, influences fibroblast adhesion and motility. TIRF microscopy reveals a dynamic population of CaMK-II at the cell surface in migrating cells. Inhibition of CaMK-II with two mechanistically distinct, membrane permeant inhibitors (KN-93 and myr-AIP) freezes lamellipodial dynamics, accelerates spreading on fibronectin, enlarges paxillin-containing focal adhesions and blocks cell motility. In contrast, constitutively active CaMK-II is not found at the cell surface, reduces cell attachment, eliminates paxillin from focal adhesions and decreases the phospho-tyrosine levels of both FAK and paxillin; all of these events can be reversed with myr-AIP. Thus, both CaMK-II inhibition and constitutive activation block cell motility through over-stabilization or destabilization of focal adhesions, respectively. Coupled with the existence of transient Ca2+ elevations and a dynamic CaMK-II population, these findings provide the first direct evidence that CaMK-II enables cell motility by transiently and locally stimulating tyrosine dephosphorylation of focal adhesion proteins to promote focal adhesion turnover.

Indexed as

AnimalsBenzenesulfonamidesBenzylaminesCalcium-Calmodulin-Dependent Protein KinasesCell MovementFibronectinsFocal Adhesion Protein-Tyrosine KinasesFocal AdhesionsImmunoblottingMiceMicroscopy, FluorescenceNIH 3T3 CellsPaxillinPhosphoproteinsProtein Kinase InhibitorsSulfonamidesBenzenesulfonamidesBenzylaminesCalcium-Calmodulin-Dependent Protein KinasesFibronectinsFocal Adhesion Protein-Tyrosine KinasesKN 93PaxillinPhosphoproteinsProtein Kinase InhibitorsSulfonamidesTyrosine

Identifiers

PMID18613116
PMCPMC2830206
OpenAlexW2117554463

What OpenQuestion holds

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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.