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N-Linked Glycosylation of the α-Amino-3-Hydroxy-5-Methylisoxazole-4-Propionate(AMPA)-Selective Glutamate Receptor Channel α2 Subunit Is Essential for the Acquisition of Ligand-Binding Activity by Susumu Kawamoto; Satoshi Hattori; Kenji Sakimura; Masayoshi Mishina; Kenji Okuda is a Neuroscience article available to read on EtoBox.

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Abstract: The N‐linked glycosylation of the α2 subunit of the mouse α‐amino‐3‐hydroxy‐5‐methylisoxazole‐4‐propionate(AMPA)‐selective glutamate receptor (GluR) channel was characterized. The receptor subunit protein has five putative __N__‐glycosylation sites. The recombinant receptor proteins were identified by [^35^S]methionine/[^35^S]cysteine metabolic labeling, western blot analysis, immunocytochemical detection, and [^3^H]AMPA binding experiments when expressed in insect __Spodoptera frugiperda__ cells using a baculovirus system. The effect of tunicamycin on the metabolic labeling and immunoblots suggested that the two products, a major protein species of ∼102 kDa and a minor species of ∼98 kDa, correspond to glycosylated and unglycosylated forms, respectively, which was also supported by the enzymic deglycosylation experiments. Immunofluorescence staining of tunicamycin‐treated cells expressing only the unglycosylated form differed little from that of tunicamycin‐nontreated cells expressing both glycosylated and unglycosylated forms. The lack of AMPA‐binding activity of the unglycosylated form expressed in the presence of tunicamycin suggested that __N__‐glycosylation is requi

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Author

Susumu Kawamoto; Satoshi Hattori; Kenji Sakimura; Masayoshi Mishina; Kenji Okuda

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)

Published

1995

Language

EN

Field

Neuroscience (Life Sciences)