AMPA receptors commandeer an ancient cargo exporter for use as an auxiliary 
subunit for signaling

Harmel, Nadine; Cokic, Barbara; Zolles, Gerd; Berkefeld, Henrike; Mauric, Veronika; Fakler, Bernd; Stein, Valentin; Kloecker, Nikolaj

doi:10.1371/journal.pone.0030681

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

AMPA receptors commandeer an ancient cargo exporter for use as an auxiliary subunit for signaling

MPS-Authors

/persons/resource/persons38792

Cokic, Barbara
Max Planck Research Group: Synaptic Receptor Trafficking / Stein, MPI of Neurobiology, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

journal.pone.0030681.pdf
(全文テキスト（全般）), 465KB

付随資料 (公開)

There is no public supplementary material available

引用

Harmel, N., Cokic, B., Zolles, G., Berkefeld, H., Mauric, V., Fakler, B., Stein, V., & Kloecker, N. (2012). AMPA receptors commandeer an ancient cargo exporter for use as an auxiliary subunit for signaling. PLoS One, 7(1):. doi:10.1371/journal.pone.0030681.

引用: https://hdl.handle.net/11858/00-001M-0000-000F-8597-A

要旨

Fast excitatory neurotransmission in the mammalian central nervous
system is mainly mediated by ionotropic glutamate receptors of the AMPA
subtype (AMPARs). AMPARs are protein complexes of the pore-lining
alpha-subunits GluA1-4 and auxiliary beta-subunits modulating their
trafficking and gating. By a proteomic approach, two homologues of the
cargo exporter cornichon, CNIH-2 and CNIH-3, have recently been
identified as constituents of native AMPARs in mammalian brain. In
heterologous reconstitution experiments, CNIH-2 promotes surface
expression of GluAs and modulates their biophysical properties.
However, its relevance in native AMPAR physiology remains
controversial. Here, we have studied the role of CNIH-2 in GluA
processing both in heterologous cells and primary rat neurons. Our data
demonstrate that CNIH-2 serves an evolutionarily conserved role as a
cargo exporter from the endoplasmic reticulum (ER). CNIH-2 cycles
continuously between ER and Golgi complex to pick up cargo protein in
the ER and then to mediate its preferential export in a coat protein
complex (COP) II dependent manner. Interaction with GluA subunits
breaks with this ancestral role of CNIH-2 confined to the early
secretory pathway. While still taking advantage of being exported
preferentially from the ER, GluAs recruit CNIH-2 to the cell surface.
Thus, mammalian AMPARs commandeer CNIH-2 for use as a bona fide
auxiliary subunit that is able to modify receptor signaling.