ArticleThe FEBS journal2016
Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate.
Article in The FEBS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
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- Investigating Protein-Glycosaminoglycan Interactions Using Paramagnetic Glycosaminoglycan Oligosaccharides.Methods in molecular biology (Clifton, N.J.) · 2025Article
- αStructure (London, England : 1993) · 2024Article
- αbioRxiv : the preprint server for biology · 2024Article
- Pleiotrophin drives a prometastatic immune niche in breast cancer.The Journal of experimental medicine · 2023Article
- Protein Tyrosine Phosphatase Receptor Zeta 1 as a Potential Target in Cancer Therapy and Diagnosis.International journal of molecular sciences · 2023Review
- Pleiotrophin Interaction with Synthetic Glycosaminoglycan Mimetics.Pharmaceuticals (Basel, Switzerland) · 2022Article
- The Interaction between Chondroitin Sulfate and Dermatan Sulfate Tetrasaccharides and Pleiotrophin.International journal of molecular sciences · 2022Article
- Antimicrobial Proteins and Peptides in Avian Eggshell: Structural Diversity and Potential Roles in Biomineralization.Frontiers in immunology · 2022Review
- Article
- Pleiotrophin interacts with glycosaminoglycans in a highly flexible and adaptable manner.FEBS letters · 2021Article
- Structural Characterization of the Interaction between the αBiochemistry · 2021Article
- Chondroitin Sulfate/Dermatan Sulfate-Protein Interactions and Their Biological Functions in Human Diseases: Implications and Analytical Tools.Frontiers in cell and developmental biology · 2021Review
- NMR Characterization of the Interactions Between Glycosaminoglycans and Proteins.Frontiers in molecular biosciences · 2021Review
- Cortical Transplantation of Brain-Mimetic Glycosaminoglycan Scaffolds and Neural Progenitor Cells Promotes Vascular Regeneration and Functional Recovery after Ischemic Stroke in Mice.Advanced healthcare materials · 2020Article
- Pleiotrophin: Activity and mechanism.Advances in clinical chemistry · 2020Review
- The carboxy-terminus, a key regulator of protein function.Critical reviews in biochemistry and molecular biology · 2019Review
- The Expression, Functions, Interactions and Prognostic Values of PTPRZ1: A Review and Bioinformatic Analysis.Journal of Cancer · 2019Review
- Pleiotrophin, a multifunctional cytokine and growth factor, induces leukocyte responses through the integrin Mac-1.The Journal of biological chemistry · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
unlabelledPleiotrophin (PTN) is a potent glycosaminoglycan-binding cytokine that is important in neural development, angiogenesis and tissue regeneration. Much of its activity is attributed to its interactions with the chondroitin sulfate (CS) proteoglycan, receptor type protein tyrosine phosphatase ζ (PTPRZ). However, there is little high resolution structural information on the interactions between PTN and CS, nor is it clear why the C-terminal tail of PTN is necessary for signaling through PTPRZ, even though it does not contribute to heparin binding. We determined the first structure of PTN and analyzed its interactions with CS. Our structure shows that PTN possesses large basic surfaces on both of its structured domains and also that residues in the hinge segment connecting the domains have significant contacts with the C-terminal domain. Our analysis of PTN-CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ. These results offer the first possible explanation of why truncated PTN missing the C-terminal tail is unable to signal through PTPRZ. NMR analysis of the interactions of PTN with CS revealed that the C-terminal domain and hinge of PTN make up the major CS-binding site in PTN, and that removal of the C-terminal tail weakened the affinity of the site for CSA but not for other high sulfation density CS. DATABASE: Coordinates of the ensemble of ten PTN structures have been deposited in RCSB under accession number 2n6f. Chemical shifts assignments and structural constraints have been deposited in BMRB under accession number 25762.
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