ArticleMolecular biology of the cell1999
Cytoskeletal reorganization induced by engagement of the NG2 proteoglycan leads to cell spreading and migration.
Article in Molecular biology of the cell, 1999. 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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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.
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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.
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Who cites it
35 citing papers in PubMed, 86 citations in OpenAlex.
- Proteolytic remodelling of the extracellular matrix by pericytes.The FEBS journal · 2026Review
- CSPG4-dependent cytotoxicity formSphere · 2024Article
- NG2/CSPG4 attenuates motility in mandibular fibrochondrocytes under serum starvation conditions.Frontiers in cell and developmental biology · 2023Article
- Cell surface chondroitin sulphate proteoglycan 4 (CSPG4) binds to the basement membrane heparan sulphate proteoglycan, perlecan, and is involved in cell adhesion.Journal of biochemistry · 2018Article
- Article
- CSPG4: a prototype oncoantigen for translational immunotherapy studies.Journal of translational medicine · 2017Review
- Subventricular zone involvement in Glioblastoma - A proteomic evaluation and clinicoradiological correlation.Scientific reports · 2017Article
- NG2 Proteoglycan Enhances Brain Tumor Progression by Promoting Beta-1 Integrin Activation in both Cis and Trans Orientations.Cancers · 2017Review
- The cytoskeletal arrangements necessary to neurogenesis.Oncotarget · 2016Review
- Stonin1 mediates endocytosis of the proteoglycan NG2 and regulates focal adhesion dynamics and cell motility.Nature communications · 2015Article
- Cytogenesis in the adult monkey motor cortex: perivascular NG2 cells are the major adult born cell type.The Journal of comparative neurology · 2015Article
- Proteoglycans in Normal and Healing Skin.Advances in wound care · 2015Article
- Transduction of extracellular cues into cell polarity: the role of the transmembrane proteoglycan NG2.Molecular neurobiology · 2014Review
- Regulation of oligodendrocyte precursor migration during development, in adulthood and in pathology.Cellular and molecular life sciences : CMLS · 2013Review
- NG2/CSPG4-collagen type VI interplays putatively involved in the microenvironmental control of tumour engraftment and local expansion.Journal of molecular cell biology · 2013Article
- NG2 cells, a new trail for Alzheimer's disease mechanisms?Acta neuropathologica communications · 2013Article
- CSPG4 protein as a new target for the antibody-based immunotherapy of triple-negative breast cancer.Journal of the National Cancer Institute · 2010Article
- Epitope distance to the target cell membrane and antigen size determine the potency of T cell-mediated lysis by BiTE antibodies specific for a large melanoma surface antigen.Cancer immunology, immunotherapy : CII · 2010Article
- NG2 cells: Properties, progeny and origin.Brain research reviews · 2010Review
- Prominent collagen type VI expression in juvenile angiofibromas.Histochemistry and cell biology · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cells expressing the NG2 proteoglycan can attach, spread, and migrate on surfaces coated with NG2 mAbs, demonstrating that engagement of NG2 can trigger the cytoskeletal rearrangements necessary for changes in cell morphology and motility. Engagement of different epitopes of the proteoglycan results in distinct forms of actin reorganization. On mAb D120, the cells contain radial actin spikes characteristic of filopodial extension, whereas on mAb N143, the cells contain cortical actin bundles characteristic of lamellipodia. Cells that express NG2 variants lacking the transmembrane and cytoplasmic domains are unable to spread or migrate on NG2 mAb-coated surfaces, indicating that these portions of the molecule are essential for NG2-mediated signal transduction. Cells expressing an NG2 variant lacking the C-terminal half of the cytoplasmic domain can still spread normally on mAbs D120 and N143, suggesting that the membrane-proximal cytoplasmic segment is responsible for this process. In contrast, this variant migrates poorly on mAb D120 and exhibits abnormal arrays of radial actin filaments decorated with fascin during spreading on this mAb. The C-terminal portion of the NG2 cytoplasmic domain, therefore, may be involved in regulating molecular events that are crucial for cell motility.
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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.