Evidence map›Paper›PMID 23806659›Full record

ArticleJournal of molecular biology2013

Structure and function of palladin's actin binding domain.

Moriah R Beck, Richard D S Dixon, Silvia M Goicoechea, Grant S Murphy, Joseph G Brungardt, Matthew T Beam, Pavan Srinath, Julie Patel, Jahan Mohiuddin, Carol A Otey and 1 more

Abstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  5. Functional comparison of full-length palladin to isolated actin binding domain.Protein science : a publication of the Protein Society · 2023
    Article
  6. Article
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  8. Review
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  10. Article
  11. The Role of Palladin in Podocytes.Journal of the American Society of Nephrology : JASN · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
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  18. Article
  19. Actin-induced dimerization of palladin promotes actin-bundling.Protein science : a publication of the Protein Society · 2015
    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

11 authors at 3 institutions in 1 country.

Moriah R BeckDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, 120 Mason Farm Road, Chapel Hill, NC 27599, USA. moriah.beck@wichita.edu
Richard D S Dixon
Silvia M Goicoechea
Grant S Murphy
Joseph G Brungardt
Matthew T Beam
Pavan Srinath
Julie Patel
Jahan Mohiuddin
Carol A Otey
Sharon L Campbell
University of North Carolina at Chapel Hill · USUNC Lineberger Comprehensive Cancer CenterWichita State University · US

Funding

TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI BANN, JAMES G. · 2002 to 2011
$20.1M
Conformational dynamics and focal adhesion kinase functionR01GM080568 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CAMPBELL, SHARON L · 2008 to 2011
$1.1M
Molecular Function of Palladin's Ig Domains in Cell Adhesion and MotilityR01GM081505 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI OTEY, CAROL A · 2009 to 2010
$370k
Elucidating the role of palladin/alpha-actinin in cell motility and invasionF32CA139926 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BECK, MORIAH R · 2009 to 2010
$59k
NCI NIH HHS F32 CA139926NCI NIH HHS F32 CA 139926-01NCRR NIH HHS P20 RR017708NIGMS NIH HHS 5R01GM080568NIGMS NIH HHS 5R01GM081505NIGMS NIH HHS R01 GM080568NIGMS NIH HHS R01 GM081505
6 · The paper itself

Abstract

Here, we report the NMR structure of the actin-binding domain contained in the cell adhesion protein palladin. Previously, we demonstrated that one of the immunoglobulin domains of palladin (Ig3) is both necessary and sufficient for direct filamentous actin binding in vitro. In this study, we identify two basic patches on opposite faces of Ig3 that are critical for actin binding and cross-linking. Sedimentation equilibrium assays indicate that the Ig3 domain of palladin does not self-associate. These combined data are consistent with an actin cross-linking mechanism that involves concurrent attachment of two actin filaments by a single palladin molecule by an electrostatic mechanism. Palladin mutations that disrupt actin binding show altered cellular distributions and morphology of actin in cells, revealing a functional requirement for the interaction between palladin and actin in vivo.

Indexed as

Protein Interaction Domains and MotifsActinsAmino Acid SubstitutionAnimalsChlorocebus aethiopsCOS CellsCytoskeletal ProteinsImmunoglobulinsMiceModels, MolecularMutagenesis, Site-DirectedPhosphoproteinsProtein BindingProtein Interaction MappingProtein TransportRabbitsActinsCytoskeletal ProteinsImmunoglobulinspalladin protein, mousePhosphoproteins3D4′,6-diamidino-2-phenylindoleABPactin binding proteinactin-binding proteincrosslinkingDAPIelectrostaticsF-actinfilamentous actinfilamin AFLNaG-actinGFPglobular or monomeric actingreen fluorescent proteinheteronuclear single quantum correlationHSQCimmunoglubulin-like domainpalladinPDBProtein Data BankRASRECresolution-adapted structural recombinationthree-dimensionalvasodilator-stimulated phosphoproteinVASP

Identifiers

PMID23806659
PMCPMC3759364
OpenAlexW2146715361

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.