ArticleJournal of cellular biochemistry2000
The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the membrane-spanning proteoglycan NG2.
Article in Journal of cellular biochemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 98 citations in OpenAlex.
- Identification of Potential Proteins Interacting with α-Galactosidase A to Analyze the Pathogenesis of Fabry Disease.International journal of molecular sciences · 2026Article
- Chondroitin Sulfate Proteoglycan 4 (CSPG4) as an Emerging Target for Immunotherapy to Treat Melanoma.Cancers · 2024Review
- Nerve-Glial antigen 2: unmasking the enigmatic cellular identity in the central nervous system.Frontiers in immunology · 2024Review
- Disrupting mechanical homeostasis promotes matrix metalloproteinase-13 mediated processing of neuron glial antigen 2 in mandibular condylar cartilage.European cells & materials · 2023Article
- Extracellular Matrix in Neural Plasticity and Regeneration.Cellular and molecular neurobiology · 2022Review
- NG2/CSPG4 regulates cartilage degeneration during TMJ osteoarthritis.Frontiers in dental medicine · 2022Article
- CSPG4 as Target for CAR-T-Cell Therapy of Various Tumor Entities-Merits and Challenges.International journal of molecular sciences · 2019Review
- The Intracellular Cleavage Product of the NG2 Proteoglycan Modulates Translation and Cell-Cycle Kinetics via Effects on mTORC1/FMRP Signaling.Frontiers in cellular neuroscience · 2018Article
- NG2 Proteoglycan Enhances Brain Tumor Progression by Promoting Beta-1 Integrin Activation in both Cis and Trans Orientations.Cancers · 2017Review
- Chondroitin Sulfate Proteoglycan 4 and Its Potential As an Antibody Immunotherapy Target across Different Tumor Types.Frontiers in immunology · 2017Review
- The regulatory mechanisms of NG2/CSPG4 expression.Cellular & molecular biology letters · 2017Review
- The Role of NG2 Proteoglycan in Glioma.Translational oncology · 2016Review
- Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for Clostridium difficile toxin B.Cell research · 2015Article
- The NG2 Proteoglycan Protects Oligodendrocyte Precursor Cells against Oxidative Stress via Interaction with OMI/HtrA2.PloS one · 2015Article
- Article
- Shedding of NG2 by MMP-13 attenuates anoikis.DNA and cell biology · 2014Article
- Transduction of extracellular cues into cell polarity: the role of the transmembrane proteoglycan NG2.Molecular neurobiology · 2014Review
- Melanoma biomolecules: independently identified but functionally intertwined.Frontiers in oncology · 2013Review
- NG2 regulates directional migration of oligodendrocyte precursor cells via Rho GTPases and polarity complex proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Proteoglycans and their roles in brain cancer.The FEBS journal · 2013Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
A yeast two-hybrid screen was employed to identify ligands for the cytoplasmic domain of the NG2 chondroitin sulfate proteoglycan. Two overlapping cDNA clones selected in the screen are identical in sequence to a DNA segment coding for the most amino-terminal of the 13 PDZ domains found in the multi-PDZ-protein MUPP1. Antibodies made against recombinant polypeptides representing these two clones (NIP-2 and NIP-7) are reactive with the same 250-kDa molecule recognized by anti-MUPP1 antibodies, confirming the presence of the NIP-2 and NIP-7 sequences in the MUPP1 protein. NIP-2 and NIP-7 GST fusion proteins effectively recognize NG2 in pull-down assays, demonstrating the ability of these polypeptide segments to interact with the intact proteoglycan. The fusion proteins fail to bind NG2 missing the C-terminal half of the cytoplasmic domain, emphasizing the role of the NG2 C-terminus in the interaction with MUPP1. The existence of an NG2/MUPP1 interaction in situ is demonstrated by the ability of NG2 antibodies to co-immunoprecipitate both NG2 and MUPP1 from detergent extracts of cells expressing the two molecules. MUPP1 may serve as a multivalent scaffold that provides a means of linking NG2 with key structural and/or signaling components in the cytoplasm.
Indexed as
Identifiers
10967549PMC3501957W2054243450What OpenQuestion holds
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.