Evidence map›Paper›PMID 26869927›Full record

ReviewFrontiers in pharmacology2016

Syndecans as Cell Surface Receptors in Cancer Biology. A Focus on their Interaction with PDZ Domain Proteins.

Bill Cheng, Marine Montmasson, Laurent Terradot, Patricia Rousselle

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in pharmacology, 2016. 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
3.0field-weighted citation impact, top 10% 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, 45 citations in OpenAlex.

  1. Article
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  16. Review
  17. Proteoglycans as Mediators of Cancer Tissue Mechanics.Frontiers in cell and developmental biology · 2020
    Review
  18. 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

4 authors at 1 institution in 1 country.

Bill ChengLaboratoire de Biologie Tissulaire et Ingénierie Thérapeutique, UMR 5305, CNRS, Institut de Biologie et Chimie des Protéines, SFR BioSciences Gerland-Lyon Sud, Université Lyon 1 Lyon, France.
Marine MontmassonLaboratoire de Biologie Tissulaire et Ingénierie Thérapeutique, UMR 5305, CNRS, Institut de Biologie et Chimie des Protéines, SFR BioSciences Gerland-Lyon Sud, Université Lyon 1 Lyon, France.
Laurent TerradotBases Moléculaires et Structurales des Systèmes Infectieux UMR 5086, CNRS, Institut de Biologie et Chimie des Protéines, SFR BioSciences Gerland-Lyon Sud, Université Lyon 1 Lyon, France.
Patricia RousselleLaboratoire de Biologie Tissulaire et Ingénierie Thérapeutique, UMR 5305, CNRS, Institut de Biologie et Chimie des Protéines, SFR BioSciences Gerland-Lyon Sud, Université Lyon 1 Lyon, France.
Université Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Syndecans are transmembrane receptors with ectodomains that are modified by glycosaminoglycan chains. The ectodomains can interact with a wide variety of molecules, including growth factors, cytokines, proteinases, adhesion receptors, and extracellular matrix (ECM) components. The four syndecans in mammals are expressed in a development-, cell-type-, and tissue-specific manner and can function either as co-receptors with other cell surface receptors or as independent adhesion receptors that mediate cell signaling. They help regulate cell proliferation and migration, angiogenesis, cell/cell and cell/ECM adhesion, and they may participate in several key tumorigenesis processes. In some cancers, syndecan expression regulates tumor cell proliferation, adhesion, motility, and other functions, and may be a prognostic marker for tumor progression and patient survival. The short cytoplasmic tail is likely to be involved in these events through recruitment of signaling partners. In particular, the conserved carboxyl-terminal EFYA tetrapeptide sequence that is present in all syndecans binds to some PDZ domain-containing proteins that may function as scaffold proteins that recruit signaling and cytoskeletal proteins to the plasma membrane. There is growing interest in understanding these interactions at both the structural and biological levels, and recent findings show their high degree of complexity. Parameters that influence the recruitment of PDZ domain proteins by syndecans, such as binding specificity and affinity, are the focus of active investigations and are important for understanding regulatory mechanisms. Recent studies show that binding may be affected by post-translational events that influence regulatory mechanisms, such as phosphorylation within the syndecan cytoplasmic tail.

Indexed as

cancercytoskeletonextracellular matrixPDZ domainphosphorylationsyndecan

Identifiers

PMID26869927
PMCPMC4735372
OpenAlexW2290411490

What OpenQuestion holds

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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.