ArticleThe Journal of cell biology1999
Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 papers.
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Who cites it
195 citing papers in PubMed, 532 citations in OpenAlex.
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- Intracranial inflammation and meningeal fibrosis are associated with perivascular changes, altered CSF tracer dynamics, and cognitive decline in a rat model of communicating hydrocephalus.Fluids and barriers of the CNS · 2026Article
- Article
- A key role of Canoe's intrinsically disordered region in linking cell junctions to the cytoskeleton.The Journal of cell biology · 2025Article
- Circadian clock proteins BMAL1 and CLOCK regulate HSV-1 entry into nerve cells through NECTIN-1.Virology journal · 2025Article
- PAK4 promotes vertex remodeling to maintain epithelial integrity and barrier function.bioRxiv : the preprint server for biology · 2025Article
- α-catenin phosphorylation is actomyosin-sensitive and required for epithelial barrier functions through Afadin.bioRxiv : the preprint server for biology · 2025Article
- Nectin4-targeted molecular imaging in solid tumors: Current status and future perspectives.View (Beijing, China) · 2025Article
- Proximity proteomics provides a new resource for exploring the function of Afadin and the complexity of cell-cell adherens junctions.Biology open · 2025Article
- EphA2 regulates vascular permeability and prostate cancer metastasis via modulation of cell junction protein phosphorylation.Oncogene · 2025Article
- Proximity proteomics provides a new resource for exploring the function of Afadin and the complexity of cell-cell adherens junctions.bioRxiv : the preprint server for biology · 2024Article
- Damaging Mutations inThe Cleft palate-craniofacial journal : official publication of the American Cleft Palate-Craniofacial Association · 2024Article
- Adherens junctions as molecular regulators of emergent tissue mechanics.Nature reviews. Molecular cell biology · 2024Review
- Too old for hide-and-seek; cell maturation reveals hidden apical junctional organization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Dilute domain in Canoe is not essential for linking cell junctions to the cytoskeleton but supports morphogenesis robustness.Journal of cell science · 2024Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Association of connexin36 with adherens junctions at mixed synapses and distinguishing electrophysiological features of those at mossy fiber terminals in rat ventral hippocampus.International journal of physiology, pathophysiology and pharmacology · 2024Article
- The Nectin family ligands, PVRL2 and PVR, in cancer immunology and immunotherapy.Frontiers in immunology · 2024Review
- Therapeutic prospects of nectin-4 in cancer: applications and value.Frontiers in oncology · 2024Review
135 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have isolated a novel actin filament-binding protein, named afadin, localized at cadherin-based cell-cell adherens junctions (AJs) in various tissues and cell lines. Afadin has one PDZ domain, three proline-rich regions, and one actin filament-binding domain. We found here that afadin directly interacted with a family of the immunoglobulin superfamily, which was isolated originally as the poliovirus receptor-related protein (PRR) family consisting of PRR1 and -2, and has been identified recently to be the alphaherpes virus receptor. PRR has a COOH-terminal consensus motif to which the PDZ domain of afadin binds. PRR and afadin were colocalized at cadherin-based cell-cell AJs in various tissues and cell lines. In E-cadherin-expressing EL cells, PRR was recruited to cadherin-based cell-cell AJs through interaction with afadin. PRR showed Ca2+-independent cell-cell adhesion activity. These results indicate that PRR is a cell-cell adhesion molecule of the immunoglobulin superfamily which is recruited to cadherin-based cell-cell AJs through interaction with afadin. We rename PRR as nectin (taken from the Latin word "necto" meaning "to connect").
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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.