Evidence map›Paper›PMID 16280362›Full record

ArticleMolecular biology of the cell2006

Proteolysis of cortactin by calpain regulates membrane protrusion during cell migration.

Benjamin J Perrin, Kurt J Amann, Anna Huttenlocher

Open access · greenAbstract 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 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

59 citing papers in PubMed, 115 citations in OpenAlex.

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  8. CaJournal of extracellular vesicles · 2020
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  9. On the cause of sleep: Protein fragments, the concept of sentinels, and links to epilepsy.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  10. Article
  11. Effects of nuclear factor I phosphorylation on calpastatin (The Journal of biological chemistry · 2019
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  12. Review
  13. Article
  14. Endothelial cell calpain as a critical modulator of angiogenesis.Biochimica et biophysica acta. Molecular basis of disease · 2017
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  15. Review
  16. Article
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  19. SDF1 reduces interneuron leading process branching through dual regulation of actin and microtubules.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
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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

3 authors at 1 institution in 1 country.

Benjamin J PerrinCellular and Molecular Biology Program, University of Wisconsin-Madison, Madison, WI 53706, USA.
Kurt J Amann
Anna Huttenlocher
University of Wisconsin–Madison · US

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
ADHESIVE REGULATION DURING CELL MIGRATIONR01CA085862 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI Anna Huttenlocher · 2000 to 2026
$7.3M
NCI NIH HHS R01 CA085862NCI NIH HHS R01CA85862-01NIGMS NIH HHS T32 GM007215NIGMS NIH HHS T32GM07215-25
6 · The paper itself

Abstract

Calpain 2 regulates membrane protrusion during cell migration. However, relevant substrates that mediate the effects of calpain on protrusion have not been identified. One potential candidate substrate is the actin binding protein cortactin. Cortactin is a Src substrate that drives actin polymerization by activating the Arp2/3 complex and also stabilizes the cortical actin network. We now provide evidence that proteolysis of cortactin by calpain 2 regulates membrane protrusion dynamics during cell migration. We show that cortactin is a calpain 2 substrate in fibroblasts and that the preferred cleavage site occurs in a region between the actin binding repeats and the alpha-helical domain. We have generated a mutant cortactin that is resistant to calpain proteolysis but retains other biochemical properties of cortactin. Expression of the calpain-resistant cortactin, but not wild-type cortactin, impairs cell migration and increases transient membrane protrusion, suggesting that calpain proteolysis of cortactin limits membrane protrusions and regulates migration in fibroblasts. Furthermore, the enhanced protrusion observed with the calpain-resistant cortactin requires both the Arp2/3 binding site and the Src homology 3 domain of cortactin. Together, these findings suggest a novel role for calpain-mediated proteolysis of cortactin in regulating membrane protrusion dynamics during cell migration.

Indexed as

Cell MovementActinsAmino Acid SequenceAnimalsBinding SitesCalpainCell LineCell MembraneCell Surface ExtensionsCortactinCricetinaeFibroblastsHumansKineticsMolecular Sequence DataProtein BindingActinsCalpainCortactin

Identifiers

PMID16280362
PMCPMC1345662
OpenAlexW2169865172

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.