Evidence map›Paper›PMID 21925511›Full record

ArticleJournal of molecular biology2011

Structural characterization of the interactions between palladin and α-actinin.

Moriah R Beck, Carol A Otey, Sharon L Campbell

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

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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 2 institutions in 1 country.

Moriah R BeckDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
Carol A Otey
Sharon L Campbell
UNC Lineberger Comprehensive Cancer CenterUniversity of North Carolina at Chapel Hill · US

Funding

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 CA139926-01NIGMS NIH HHS 5R01GM080568NIGMS NIH HHS R01 GM080568NIGMS NIH HHS R01 GM081505NIGMS NIH HHS R01GM081505
6 · The paper itself

Abstract

The interaction between α-actinin and palladin, two actin-cross-linking proteins, is essential for proper bidirectional targeting of these proteins. As a first step toward understanding the role of this complex in organizing cytoskeletal actin, we have characterized binding interactions between the EF-hand domain of α-actinin (Act-EF34) and peptides derived from palladin and generated an NMR-derived structural model for the Act-EF34/palladin peptide complex. The critical binding site residues are similar to an α-actinin binding motif previously suggested for the complex between Act-EF34 and titin Z-repeats. The structure-based model of the Act-EF34/palladin peptide complex expands our understanding of binding specificity between the scaffold protein α-actinin and various ligands, which appears to require an α-helical motif containing four hydrophobic residues, common to many α-actinin ligands. We also provide evidence that the Family X mutation in palladin, associated with a highly penetrant form of pancreatic cancer, does not interfere with α-actinin binding.

Indexed as

ActininBinding SitesCircular DichroismCrystallography, X-RayCytoskeletal ProteinsEF Hand MotifsHumansMagnetic Resonance SpectroscopyModels, MolecularPhosphoproteinsProtein BindingProtein ConformationActininACTN2 protein, humanCytoskeletal ProteinsPALLD protein, humanPhosphoproteins

Identifiers

PMID21925511
PMCPMC3226707
OpenAlexW1992677352

What OpenQuestion holds

Textmetadata
LicenceTDM
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.