Evidence map›Paper›PMID 15930135›Full record

ArticleMolecular biology of the cell2005

Functional role of syndecan-1 cytoplasmic V region in lamellipodial spreading, actin bundling, and cell migration.

Ritu Chakravarti, Vasileia Sapountzi, Josephine C Adams

Erratum issuedAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 53 citations in OpenAlex.

  1. Endothelial Surface Glycocalyx in Vascular Functions and Diseases.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Review
  4. 14-3-3ζ suppresses RANKL signaling by destabilizing TRAF6.The Journal of biological chemistry · 2024
    Article
  5. Review
  6. Article
  7. THE GLYCOCALYX AND TRAUMA: A REVIEW.Shock (Augusta, Ga.) · 2016
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Syndecan-1 modulates the motility and resolution responses of macrophages.Arteriosclerosis, thrombosis, and vascular biology · 2015
    Article
  13. Article
  14. Article
  15. Arrays of topographically and peptide-functionalized hydrogels for analysis of biomimetic extracellular matrix properties.Journal of vacuum science and technology. B, Nanotechnology & microelectronics : materials, processing, measurement, & phenomena : JVST B · 2012
    Article
  16. Article
  17. Article
  18. Syndecan-1: an inhibitor of arterial smooth muscle cell growth and intimal hyperplasia.Arteriosclerosis, thrombosis, and vascular biology · 2009
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Ritu ChakravartiDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.
Vasileia Sapountzi
Josephine C Adams
Cleveland Clinic · USMRC Laboratory for Molecular Cell Biology · GB

Funding

Fascin Protrusions in ECM-Cytoskeletal NetworkingR01GM068073 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI ADAMS, JOSEPHINE C · 2003 to 2007
$1.5M
NIGMS NIH HHS GM068073NIGMS NIH HHS R01 GM068073Wellcome Trust
6 · The paper itself

Abstract

Cell protrusions contribute to cell motility and migration by mediating the outward extension and initial adhesion of cell edges. In many cells, these extensions are supported by actin bundles assembled by the actin cross-linking protein, fascin. Multiple extracellular cues regulate fascin and here we focus on the mechanism by which the transmembrane proteoglycan, syndecan-1, specifically activates lamellipodial cell spreading and fascin-and-actin bundling when clustered either by thrombospondin-1, laminin, or antibody to the syndecan-1 extracellular domain. There is almost no knowledge of the signaling mechanisms of syndecan-1 cytoplasmic domain and we have tested the hypothesis that the unique V region of syndecan-1 cytoplasmic domain has a crucial role in these processes. By four criteria--the activities of N-cadherin/V region chimeras, syndecan-1 deletion mutants, or syndecan-1 point mutants, and specific inhibition by a membrane-permeable TAT-V peptide--we demonstrate that the V region is necessary and sufficient for these cell behaviors and map the molecular basis for its activity to multiple residues located across the V region. These activities correlate with a V-region-dependent incorporation of cell-surface syndecan-1 into a detergent-insoluble form. We also demonstrate functional roles of syndecan-1 V region in laminin-dependent C2C12 cell adhesion and three-dimensional cell migration. These data identify for the first time specific cell behaviors that depend on signaling through the V region of syndecan-1.

Indexed as

Cell MovementActinsAmino Acid SequenceAnimalsCarrier ProteinsCell AdhesionCell LineChlorocebus aethiopsCytoplasmCytoskeletonExtracellular MatrixHumansLigandsMembrane GlycoproteinsMiceMicrofilament ProteinsActinsCarrier ProteinsfascinLigandsMembrane GlycoproteinsMicrofilament ProteinsPeptide FragmentsProteoglycansSDC1 protein, humanSdc1 protein, mouseSyndecan-1Syndecans

Identifiers

PMID15930135
PMCPMC1182307
OpenAlexW2171627581

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.