Evidence map›Paper›PMID 16987960›Full record

ArticleMolecular biology of the cell2006

Myristoylated, alanine-rich C-kinase substrate phosphorylation regulates growth cone adhesion and pathfinding.

Jesse C Gatlin, Adriana Estrada-Bernal, Staci D Sanford, Karl H Pfenninger

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 60 citations in OpenAlex.

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  16. MARCKS protein mediates hydrogen peroxide regulation of endothelial permeability.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. MARCKS regulates growth and radiation sensitivity and is a novel prognostic factor for glioma.Clinical cancer research : an official journal of the American Association for Cancer Research · 2012
    Article
  18. Article
  19. Article
  20. Growth cones as soft and weak force generators.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

4 authors at 1 institution in 1 country.

Jesse C GatlinDepartment of Pediatrics, University of Colorado School of Medicine, University of Colorado Cancer Center, Aurora, CO 80045, USA.
Adriana Estrada-Bernal
Staci D Sanford
Karl H Pfenninger
University of Colorado Cancer Center · US

Funding

EICOSANOID IN GROWTH CONE REPELLENT SIGNALINGR01NS041029 · NINDS · UNIVERSITY OF COLORADO DENVER · PI PFENNINGER, KARL H · 2001 to 2005
$1.5M
Modulation of Growth Cone Repellent ResponsesF31NS048710 · NINDS · UNIVERSITY OF COLORADO DENVER · PI SANFORD, STACI D · 2005 to 2008
$97k
MARCKS Phosphorylation in Growth Cone SignalingF31NS044705 · NINDS · UNIVERSITY OF COLORADO DENVER · PI GATLIN, JESSE C · 2002 to 2004
$70k
NINDS NIH HHS F31 NS044705NINDS NIH HHS F31 NS048710NINDS NIH HHS F31 NS44705NINDS NIH HHS F31 NS48710NINDS NIH HHS R01 NS041029NINDS NIH HHS R01 NS41029
6 · The paper itself

Abstract

Repellents evoke growth cone turning by eliciting asymmetric, localized loss of actin cytoskeleton together with changes in substratum attachment. We have demonstrated that semaphorin-3A (Sema3A)-induced growth cone detachment and collapse require eicosanoid-mediated activation of protein kinase C epsilon (PKC epsilon) and that the major PKC epsilon target is the myristoylated, alanine-rich C-kinase substrate (MARCKS). Here, we show that PKC activation is necessary for growth cone turning and that MARCKS, while at the membrane, colocalizes with alpha3-integrin in a peripheral adhesive zone of the growth cone. Phosphorylation of MARCKS causes its translocation from the membrane to the cytosol. Silencing MARCKS expression dramatically reduces growth cone spread, whereas overexpression of wild-type MARCKS inhibits growth cone collapse triggered by PKC activation. Expression of phosphorylation-deficient, mutant MARCKS greatly expands growth cone adhesion, and this is characterized by extensive colocalization of MARCKS and alpha3-integrin, resistance to eicosanoid-triggered detachment and collapse, and reversal of Sema3A-induced repulsion into attraction. We conclude that MARCKS is involved in regulating growth cone adhesion as follows: its nonphosphorylated form stabilizes integrin-mediated adhesions, and its phosphorylation-triggered release from adhesions causes localized growth cone detachment critical for turning and collapse.

Indexed as

12-Hydroxy-5,8,10,14-eicosatetraenoic AcidActinsAnimalsCell AdhesionCytoskeletonGanglia, SpinalGene ExpressionGene SilencingGrowth ConesHumansIntegrin alpha3Intracellular Signaling Peptides and ProteinsMembrane ProteinsMyristoylated Alanine-Rich C Kinase SubstratePhosphorylationProtein Kinase C12-Hydroxy-5,8,10,14-eicosatetraenoic AcidActinsIntegrin alpha3Intracellular Signaling Peptides and ProteinsMARCKS protein, humanMarcks protein, ratMembrane ProteinsMyristoylated Alanine-Rich C Kinase SubstrateProtein Kinase CSEMA3A protein, humanSemaphorin-3ATetradecanoylphorbol Acetate

Identifiers

PMID16987960
PMCPMC1679677
OpenAlexW2107220456

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.