ArticleInternational journal of molecular sciences2018
N-Glycosylation Regulates Pannexin 2 Localization but Is Not Required for Interacting with Pannexin 1.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Pannexins in the heart: cell-specific expression and contributions to disease.Cell and tissue research · 2026Review
- Pannexins in the vasculature.American journal of physiology. Heart and circulatory physiology · 2025Review
- Pannexin channels in the kidney.American journal of physiology. Renal physiology · 2025Review
- Pannexin channels in inflammation and tumorigenesis.Frontiers in cell and developmental biology · 2025Review
- Pannexin 2 is expressed in murine skin and promotes UVB-induced apoptosis of keratinocytes.Molecular biology of the cell · 2022Article
- Article
- Alternative neural systems: What is a neuron? (Ctenophores, sponges and placozoans).Frontiers in cell and developmental biology · 2022Article
- Pannexin 1 mutation found in melanoma tumor reduces phosphorylation, glycosylation, and trafficking of the channel-forming protein.Molecular biology of the cell · 2021Article
- Silencing GnT-V reduces oxaliplatin chemosensitivity in human colorectal cancer cells through N-glycan alteration of organic cation transporter member 2.Experimental and therapeutic medicine · 2021Article
- Identification and classification of innexin gene transcripts in the central nervous system of the terrestrial slug Limax valentianus.PloS one · 2021Article
- Pannexin-1 Channel Regulates ATP Release in Epilepsy.Neurochemical research · 2020Review
- A novel motif in the proximal C-terminus of Pannexin 1 regulates cell surface localization.Scientific reports · 2019Article
- An Overview of the Focus of the International Gap Junction Conference 2017 and Future Perspectives.International journal of molecular sciences · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues. We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown. Panx1 and Panx2 intermixing can regulate channel properties, and both pannexins have been implicated in neuronal cell death after ischemia. Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1. We used site-directed mutagenesis, enzymatic de-glycosylation, cell-surface biotinylation, co-immunoprecipitation, and confocal microscopy. Our results showed that N86 is the only N-glycosylation site of Panx2. Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1. The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1. Our study indicates that N-glycosylation may be important for folding and trafficking of Panx2. We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
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