Evidence map›Paper›PMID 17537434›Full record

ArticleExperimental cell research2007

Palladin interacts with SH3 domains of SPIN90 and Src and is required for Src-induced cytoskeletal remodeling.

Mikko Rönty, Anu Taivainen, Leena Heiska, Carol Otey, Elisabeth Ehler, Woo Keun Song, Olli Carpen

Open access · greenAbstract read
In one paragraph

Article in Experimental cell research, 2007. 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
2.2field-weighted citation impact, top 14% 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, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Functional comparison of full-length palladin to isolated actin binding domain.Protein science : a publication of the Protein Society · 2023
    Article
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  7. Review
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  12. Actin binding proteins, spermatid transport and spermiation.Seminars in cell & developmental biology · 2014
    Review
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  14. 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

7 authors at 6 institutions in 4 countries.

Mikko RöntyDepartment of Pathology, Neuroscience Program, Biomedicum Helsinki, University of Helsinki and Helsinki University Hospital, Helsinki, Finland. mikko.ronty@helsinki.fi
Anu Taivainen
Leena Heiska
Carol Otey
Elisabeth Ehler
Woo Keun Song
Olli Carpen
University of Helsinki · FIGwangju Institute of Science and Technology · KRHelsinki University Hospital · FIKing's College London · GBTurku University Hospital · FIUniversity of North Carolina at Chapel Hill · US

Funding

Role of Palladin in Regulating AstrocytesR01NS043253 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI OTEY, CAROL A · 2002 to 2006
$1.6M
Biochemical Regulation of Actin Cytoskeleton AssemblyR01GM061743 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI OTEY, CAROL A · 2002 to 2005
$1.0M
Medical Research Council G0400153NIGMS NIH HHS GM61743NIGMS NIH HHS R01 GM061743NINDS NIH HHS NS43253NINDS NIH HHS R01 NS043253
6 · The paper itself

Abstract

Palladin and SPIN90 are widely expressed proteins, which participate in modulation of actin cytoskeleton by binding to a variety of scaffold and signaling molecules. Cytoskeletal reorganization can be induced by activation of signaling pathways, including the PDGF receptor and Src tyrosine kinase pathways. In this study we have analyzed the interplay between palladin, SPIN90 and Src and characterized the role of palladin and SPIN90 in PDGF and Src-induced cytoskeletal remodeling. We show that the SH3 domains of SPIN90 and Src directly bind palladin's poly-proline sequence and the interaction controls intracellular targeting of SPIN90. In PDGF-treated cells, palladin and SPIN90 co-localize in actin-rich membrane ruffles and lamellipodia. The effect of PDGF on the cytoskeleton is at least partly mediated by the Src kinase since PP2, a selective Src kinase family inhibitor, blocked PDGF-induced changes. Furthermore, expression of active Src kinase resulted in coordinated translocation of both palladin and SPIN90 to membrane protrusions. Knock-down of endogenous SPIN90 did not inhibit Src-induced cytoskeletal rearrangement, whereas knock-down of palladin resulted in cytoskeletal disorganization and inhibition of remodeling. Further studies showed that palladin is tyrosine phosphorylated in cells expressing active Src indicating bidirectional interplay between palladin and Src. These results may have implications in understanding the invasive and metastatic phenotype of neoplastic cells induced by Src.

Indexed as

src Homology DomainsActinsAdaptor Proteins, Signal TransducingAnimalsChlorocebus aethiopsCOS CellsCytoskeletal ProteinsCytoskeletonEnzyme ActivationHumansMuscle ProteinsPhosphoproteinsPhosphorylationPhosphotyrosinePlatelet-Derived Growth FactorProtein BindingActinsAdaptor Proteins, Signal TransducingCytoskeletal ProteinsMuscle ProteinsNCKIPSD protein, humanPALLD protein, humanPhosphoproteinsPhosphotyrosinePlatelet-Derived Growth Factorsrc-Family Kinases

Identifiers

PMID17537434
PMCPMC2000818
OpenAlexW2069960138

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.