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

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

Research output: Contribution to journalArticle

182 Citations (Scopus)

Abstract

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 site-directed mutagenesis we analyzed three putative N-linked glycosylation sites and examined the effects of each mutation on channel expression. We show for the first time that Pannexin1 is glycosylated at Asn-254 and that this residue is important for plasma membrane targeting. The glycosylation of Pannexin1 at its extracellular surface makes it unlikely that two oligomers could dock to form an intercellular channel. Ultrastructural analysis by electron microscopy confirmed that Pannexin1 junctional areas do not appear as canonical gap junctions. Rather, Pannexin1 channels are distributed throughout the plasma membrane. We propose that N-glycosylation of Pannexin1 could be a significant mechanism for regulating the trafficking of these membrane proteins to the cell surface in different tissues.

Original languageEnglish
Pages (from-to)31733-31743
Number of pages11
JournalJournal of Biological Chemistry
Volume282
Issue number43
DOIs
StatePublished - Oct 26 2007

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Glycosylation
Cell membranes
Gap Junctions
Cell Membrane
Membrane Proteins
Tissue
Mutagenesis
Docks
Connexins
Neurology
Site-Directed Mutagenesis
Oligomers
Electron microscopy
Vertebrates
Electron Microscopy
Central Nervous System
Topology
Membranes
Mutation
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. / Boassa, Daniela; Ambrosi, Cinzia; Qiu, Feng; Dahl, Gerhard; Gaietta, Guido; Sosinsky, Gina.

In: Journal of Biological Chemistry, Vol. 282, No. 43, 26.10.2007, p. 31733-31743.

Research output: Contribution to journalArticle

Boassa, Daniela ; Ambrosi, Cinzia ; Qiu, Feng ; Dahl, Gerhard ; Gaietta, Guido ; Sosinsky, Gina. / Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 43. pp. 31733-31743.
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