Evidence map›Paper›PMID 24071777›Full record

ArticleNature communications2013

CARMIL leading edge localization depends on a non-canonical PH domain and dimerization.

Adam Zwolak, Changsong Yang, Elizabeth A Feeser, E Michael Ostap, Tatyana Svitkina, Roberto Dominguez

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2013. 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
2.3field-weighted citation impact, top 13% 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, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Membrane Ruffles: Composition, Function, Formation and Visualization.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Phafins Are More Than Phosphoinositide-Binding Proteins.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. A potential founder variant inMolecular genetics & genomic medicine · 2016
    Article
  18. Article
  19. Article
  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

6 authors at 1 institution in 1 country.

Adam ZwolakDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, 728 Clinical Research Building, 415 Curie Boulevard, Philadelphia, Pennsylvania 19104, USA.
Changsong Yang
Elizabeth A Feeser
E Michael Ostap
Tatyana Svitkina
Roberto Dominguez
University of Pennsylvania · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
Molecular function of Myosin-lR37GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2016 to 2025
$5.3M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
BAR PROTEINS LINKING MEMBRANE AND CYTOSKELETON DYNAMICSR01MH087950 · NIMH · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2010 to 2020
$4.0M
MOLECULAR DESIGN OF FILOPODIA, CELL'S SENSORY ORGANELLESR01GM070898 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SVITKINA, TATYANA · 2004 to 2012
$2.7M
Myosin-1 interactions with membranesF32GM090551 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI FEESER, ELIZABETH A. · 2010 to 2012
$153k
NIGMS NIH HHS F32 GM090551NIGMS NIH HHS GM057247NIGMS NIH HHS GM070898NIGMS NIH HHS GM090551NIGMS NIH HHS GM103485NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R01 GM057247NIGMS NIH HHS R01 GM070898NIGMS NIH HHS R01 GM073791NIGMS NIH HHS R37 GM057247NIGMS NIH HHS Y01 GM000080NIMH NIH HHS R01 MH087950
6 · The paper itself

Abstract

CARMIL is an approximately 1,370-amino-acid cytoskeletal scaffold that has crucial roles in cell motility and tissue development through interactions with cytoskeletal effectors and regulation of capping protein at the leading edge. However, the mechanism of CARMIL leading edge localization is unknown. Here we show that CARMIL interacts directly with the plasma membrane through its amino-terminal region. The crystal structure of CARMIL1-668 reveals that this region harbours a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain. Lipid binding is mediated by the PH domain, but is further enhanced by a central helical domain. Small-angle X-ray scattering reveals that the helical domain mediates antiparallel dimerization, properly positioning the PH domains for simultaneous membrane interaction. In cells, deletion of the PH domain impairs leading edge localization. The results support a direct membrane-binding mechanism for CARMIL localization at the leading edge, where it regulates cytoskeletal effectors and motility.

Indexed as

Amino Acid SequenceAnimalsBinding SitesBrain ChemistryCarrier ProteinsCell Line, TumorCell MembraneCell MovementCrystallography, X-RayCytoskeletonKineticsLipidsMiceMicrofilament ProteinsModels, MolecularMolecular Sequence DataCarmil1 protein, mouseCarrier ProteinsLipidsMicrofilament ProteinsRecombinant Proteins

Identifiers

PMID24071777
PMCPMC3796438
OpenAlexW2101365401

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.