ArticleThe Journal of cell biology2000
Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 146 citations in OpenAlex.
- Host E3 ubiquitin ligase ITCH mediatesmBio · 2024Article
- Host E3 ubiquitin ligase ITCH mediatesbioRxiv : the preprint server for biology · 2023Article
- The role of NEDD4 related HECT-type E3 ubiquitin ligases in defective autophagy in cancer cells: molecular mechanisms and therapeutic perspectives.Molecular medicine (Cambridge, Mass.) · 2023Review
- A GID E3 ligase assembly ubiquitinates an Rsp5 E3 adaptor and regulates plasma membrane transporters.EMBO reports · 2022Article
- ENTREP/FAM189A2 encodes a new ITCH ubiquitin ligase activator that is downregulated in breast cancer.EMBO reports · 2022Article
- Pathobiological functions and clinical implications of annexin dysregulation in human cancers.Frontiers in cell and developmental biology · 2022Review
- Functions and Molecular Mechanisms of Deltex Family Ubiquitin E3 Ligases in Development and Disease.Frontiers in cell and developmental biology · 2021Review
- ITCH as a potential therapeutic target in human cancers.Seminars in cancer biology · 2020Review
- Regulation of SH3PX1 by dNedd4-long at theThe Journal of biological chemistry · 2019Article
- E3 ubiquitin ligase Nedd4 inhibits AP-1 activity and TNF-α production through targeting p38α for polyubiquitination and subsequent degradation.Scientific reports · 2017Article
- Control of the dynamics and homeostasis of the Drosophila Hedgehog receptor Patched by two C2-WW-HECT-E3 Ubiquitin ligases.Open biology · 2015Article
- Review
- Review
- Synaptic strength is bidirectionally controlled by opposing activity-dependent regulation of Nedd4-1 and USP8.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Nedd4 is a specific E3 ubiquitin ligase for the NMDA receptor subunit GluN2D.Neuropharmacology · 2013Article
- WWP1: a versatile ubiquitin E3 ligase in signaling and diseases.Cellular and molecular life sciences : CMLS · 2012Review
- Dlg3 trafficking and apical tight junction formation is regulated by nedd4 and nedd4-2 e3 ubiquitin ligases.Developmental cell · 2011Article
- A splice isoform of DNedd4, DNedd4-long, negatively regulates neuromuscular synaptogenesis and viability in Drosophila.PloS one · 2011Article
- The ESCRT-associated protein Alix recruits the ubiquitin ligase Nedd4-1 to facilitate HIV-1 release through the LYPXnL L domain motif.Journal of virology · 2010Article
- Calcium activates Nedd4 E3 ubiquitin ligases by releasing the C2 domain-mediated auto-inhibition.The Journal of biological chemistry · 2010Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nedd4 is a ubiquitin protein ligase (E3) containing a C2 domain, three or four WW domains, and a ubiquitin ligase HECT domain. We have shown previously that the C2 domain of Nedd4 is responsible for its Ca(2+)-dependent targeting to the plasma membrane, particularly the apical region of epithelial MDCK cells. To investigate this apical preference, we searched for Nedd4-C2 domain-interacting proteins that might be involved in targeting Nedd4 to the apical surface. Using immobilized Nedd4-C2 domain to trap interacting proteins from MDCK cell lysate, we isolated, in the presence of Ca(2+), a approximately 35-40-kD protein that we identified as annexin XIII using mass spectrometry. Annexin XIII has two known isoforms, a and b, that are apically localized, although XIIIa is also found in the basolateral compartment. In vitro binding and coprecipitation experiments showed that the Nedd4-C2 domain interacts with both annexin XIIIa and b in the presence of Ca(2+), and the interaction is direct and optimal at 1 microM Ca(2+). Immunofluorescence and immunogold electron microscopy revealed colocalization of Nedd4 and annexin XIIIb in apical carriers and at the apical plasma membrane. Moreover, we show that Nedd4 associates with raft lipid microdomains in a Ca(2+)-dependent manner, as determined by detergent extraction and floatation assays. These results suggest that the apical membrane localization of Nedd4 is mediated by an association of its C2 domain with the apically targeted annexin XIIIb.
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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.