ArticleProceedings of the National Academy of Sciences of the United States of America1999
The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin 1C: a clue for a role of NOVH in cell-adhesion signaling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 147 citations in OpenAlex.
- A working model for CCN3 C-terminal domain-mediated transcriptional modulation of the plasminogen activation system.Journal of cell communication and signaling · 2026Review
- CCN3 as a moonlighting signaling protein: a potential model for dual nuclear and extracellular functions across the CCN family.Cell communication and signaling : CCS · 2026Review
- Amino-truncated NOV expression and its correlation with clinicopathologic features, prognosis, metastasis, and chemoresistance in bladder cancer.Cancer biology & therapy · 2024Article
- Novel insights into the multifaceted and tissue-specific roles of the endocytic receptor LRP1.The Journal of biological chemistry · 2024Review
- Molecular and Genetic Interactions between CCN2 and CCN3 behind Their Yin-Yang Collaboration.International journal of molecular sciences · 2022Review
- The CCN2/CTGF interactome: an approach to understanding the versatility of CCN2/CTGF molecular activities.Journal of cell communication and signaling · 2021Review
- CCN3 is dynamically regulated by treatment and disease state in multiple sclerosis.Journal of neuroinflammation · 2020Article
- Cell Derived Matrix Fibulin-1 Associates With Epidermal Growth Factor Receptor to Inhibit Its Activation, Localization and Function in Lung Cancer Calu-1 Cells.Frontiers in cell and developmental biology · 2020Article
- The concept of the CCN protein family revisited: a centralized coordination network.Journal of cell communication and signaling · 2018Review
- Periostin is required for matricellular localization of CCN3 in periodontal ligament of mice.Journal of cell communication and signaling · 2017Article
- Dual roles of CCN proteins in breast cancer progression.Journal of cell communication and signaling · 2016Article
- Emerging role of CCN family proteins in tumorigenesis and cancer metastasis (Review).International journal of molecular medicine · 2015Review
- Article
- Expansion of melanoma-specific lymphocytes in alternate gamma chain cytokines: gene expression variances between T cells and T-cell subsets exposed to IL-2 versus IL-7/15.Cancer gene therapy · 2014Article
- The role of the CCN family of proteins in female reproduction.Cellular and molecular life sciences : CMLS · 2014Review
- CCN proteins: A centralized communication network.Journal of cell communication and signaling · 2013Article
- Dysfunction of collagen synthesis and secretion in chondrocytes induced by wisp3 mutation.International journal of endocrinology · 2013Article
- Hemicentin 2 and Fibulin 1 are required for epidermal-dermal junction formation and fin mesenchymal cell migration during zebrafish development.Developmental biology · 2012Article
- CCN3 modulates bone turnover and is a novel regulator of skeletal metastasis.Journal of cell communication and signaling · 2012Article
- Roles for CCN2 in normal physiological processes.Cellular and molecular life sciences : CMLS · 2011Review
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
The NOVH protein belongs to the emerging CCN [Connective tissue growth factor (CTGF), Cyr61/Cef10, nephroblastoma overexpressed gene] family of growth regulators sharing a strikingly conserved multimodular organization but exhibiting distinctive functional features. Two members of the family (CYR61 and CTGF) are positive regulators of cell proliferation, whereas NOVH and two other members (ELM1 and RCOP-1) exhibit features of negative regulators of growth. The multimodular structure of these proteins suggests that their biological role(s) may depend on interactions with several factors as well as proteins constitutive of the extracellular matrix. To gain insight into the functionality of these domains, we have used a two-hybrid system to identify proteins interacting with NOVH. We report here that the C-terminal domain confers on the full-length NOVH protein the capacity to bind fibulin 1C, a protein of the extracellular matrix that interacts with several other regulators of cell adhesion. Furthermore, we show that a natural N-truncated isoform of NOVH produced by cells expressing the full-length NOVH protein also binds fibulin 1C with a high affinity, and we hypothesize that the production of truncated isoforms of NOVH (and probably of other CCN proteins) may be a critical aspect in the modulation of their biological activity. These results set the stage for a study of NOVH-fibulin 1C interactions and their potential significance in cell-adhesion signaling in normal and pathological conditions.
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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.