ArticleThe Journal of biological chemistry2009
Tyrosine dephosphorylation of the syndecan-1 PDZ binding domain regulates syntenin-1 recruitment.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Syntenin inhibition impairs stroma-tumor communication in multiple myeloma and improves bortezomib treatment efficiency.HemaSphere · 2025Article
- Article
- Biology of the Heparanase-Heparan Sulfate Axis and Its Role in Disease Pathogenesis.Seminars in thrombosis and hemostasis · 2021Review
- Interplay between Cell-Surface Receptors and Extracellular Matrix in Skin.Biomolecules · 2020Review
- Proteoglycans as Mediators of Cancer Tissue Mechanics.Frontiers in cell and developmental biology · 2020Review
- Syntenin: PDZ Protein Regulating Signaling Pathways and Cellular Functions.International journal of molecular sciences · 2019Review
- Conformational Dynamics and Cooperativity Drive the Specificity of a Protein-Ligand Interaction.Biophysical journal · 2019Article
- Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition.International review of cell and molecular biology · 2019Review
- Dually modified transmembrane proteoglycans in development and disease.Cytokine & growth factor reviews · 2018Review
- Effects of syndecan-1 on the expression of syntenin and the migration of U251 glioma cells.Oncology letters · 2017Article
- The RING finger- and PDZ domain-containing protein PDZRN3 controls localization of the MgThe Journal of biological chemistry · 2017Article
- PRMT5 C-terminal Phosphorylation Modulates a 14-3-3/PDZ Interaction Switch.The Journal of biological chemistry · 2017Article
- Insights into the C-terminal Peptide Binding Specificity of the PDZ Domain of Neuronal Nitric-oxide Synthase: CHARACTERIZATION OF THE INTERACTION WITH THE TIGHT JUNCTION PROTEIN CLAUDIN-3.The Journal of biological chemistry · 2016Article
- Syndecans as Cell Surface Receptors in Cancer Biology. A Focus on their Interaction with PDZ Domain Proteins.Frontiers in pharmacology · 2016Review
- Motif co-regulation and co-operativity are common mechanisms in transcriptional, post-transcriptional and post-translational regulation.Cell communication and signaling : CCS · 2015Review
- Cytoplasmic domain interactions of syndecan-1 and syndecan-4 with α6β4 integrin mediate human epidermal growth factor receptor (HER1 and HER2)-dependent motility and survival.The Journal of biological chemistry · 2014Article
- Elevated expression of syntenin in breast cancer is correlated with lymph node metastasis and poor patient survival.Breast cancer research : BCR · 2013Article
- Syndecan-4 phosphorylation is a control point for integrin recycling.Developmental cell · 2013Article
- The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics.Structure (London, England : 1993) · 2013Article
- Syndecan and integrin interactomes: large complexes in small spaces.Current opinion in structural biology · 2012Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heparan sulfate proteoglycan receptor syndecan-1 interacts with the carboxyl-terminal LG4/5 domain in laminin 332 (alpha3LG4/5) and participates in cell adhesion and spreading. To dissect the function of syndecan-1 in these processes, we made use of a cell adhesion model in which syndecan-1 exclusively interacts with a recombinantly expressed alpha3LG4/5 fragment. Plating HT1080 cells on this fragment induces the formation of actin-containing protrusive structures in an integrin-independent manner. Here we show that syndecan-1-mediated formation of membrane protrusions requires dephosphorylation of tyrosine residues in syndecan-1. Accordingly, inhibition of phosphatases with orthovanadate decreases cell adhesion to the alpha3LG4/5 fragment. We demonstrate that the PDZ-containing protein syntenin-1, known to connect cytoskeletal proteins, binds to syndecan-1 in cells plated on the alpha3LG4/5 fragment and participates in the formation of membrane protrusions. We further show that syntenin-1 recruitment depends on the dephosphorylation of Tyr-309 located within syndecan-1 PDZ binding domain EFYA. We propose that tyrosine dephosphorylation of syndecan-1 may regulate its association with cytoskeleton components.
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Registered trials
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.