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Article

Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane.

The Journal of biological chemistry - 26 Oct 2007

Boassa Daniela, Ambrosi Cinzia, Qiu Feng, Dahl Gerhard, Gaietta Guido, Sosinsky Gina

Abstract excerpt

Pannexins are newly discovered channel proteins expressed in many different tissues and abundantly in the vertebrate central nervous system. Based on membrane topology, folding and secondary structure prediction, pannexins are proposed to form gap junction-like structures. We show here that Pannexin1 forms a hexameric channel and reaches the cell surface but, unlike connexins, is N-glycosylated. Using...

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Identifiers

PMID: 17715132
DOI: 10.1074/jbc.M702422200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane.PMID 17715132Read ↗

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A Germline Variant in the PANX1 Gene Has Reduced Channel Function and Is Associated with Multisystem DysfunctionSemantic proximity Read ↗

Pannexins, a family of gap junction proteins expressed in brainSemantic proximity Read ↗

Connexins: Synthesis, Post-Translational Modifications and Trafficking in Health and DiseaseSemantic proximity Read ↗

Identification and characterization of site-specific N-glycosylation in the potassium channel Kv3.1b.Semantic proximity Read ↗

N-glycosylation of the AMPA-type glutamate receptor regulates cell surface expression and tetramer formation affecting channel function.Semantic proximity Read ↗

The Pannexin1 membrane channel: distinct conformations and functions.Semantic proximity Read ↗

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