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Golgi Anti-apoptotic Proteins Are Highly Conserved Ion Channels That Affect Apoptosis and Cell Migration


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Publication Date: 2015-02-24

Journal Title: Journal of Biological Chemistry

Publisher: American Society for Biochemistry and Molecular Biology

Volume: 290

Pages: 11785-11801

Language: English

Type: Article

Metadata: Show full item record

Citation: Carrara, G., Saraiva, N., Parsons, M., Byrne, B., Prole, D. L., Taylor, C. W., & Smith, G. L. (2015). Golgi Anti-apoptotic Proteins Are Highly Conserved Ion Channels That Affect Apoptosis and Cell Migration. Journal of Biological Chemistry, 290 11785-11801.

Description: This is the final published version. It first appeared at http://www.jbc.org/content/290/18/11785.long.

Abstract: Golgi anti-apoptotic proteins (GAAPs) are multitransmembrane proteins that are expressed in the Golgi apparatus and are able to homo-oligomerize. They are highly conserved throughout eukaryotes and are present in some prokaryotes and orthopoxviruses. Within eukaryotes, GAAPs regulate the Ca2+ content of intracellular stores, inhibit apoptosis, and promote cell adhesion and migration. Data presented here demonstrate that purified viral GAAPs (vGAAPs) and human Bax inhibitor 1 form ion channels and that vGAAP from camelpox virus is selective for cations. Mutagenesis of vGAAP, including some residues conserved in the recently solved structure of a related bacterial protein, BsYetJ, altered the conductance (E207Q and D219N) and ion selectivity (E207Q) of the channel. Mutation of residue Glu-207 or -178 reduced the effects of GAAP on cell migration and adhesion without affecting protection from apoptosis. In contrast, mutation of Asp-219 abrogated the anti-apoptotic activity of GAAP but not its effects on cell migration and adhesion. These results demonstrate that GAAPs are ion channels and define residues that contribute to the ion-conducting pore and affect apoptosis, cell adhesion, and migration independently.

Sponsorship: This work was supported by the United Kingdom Medical Research Council, the Biotechnology and Biological Sciences Research Council, and the Wellcome Trust.

Identifiers:

This record's URL: http://dx.doi.org/10.1074/jbc.M115.637306http://www.repository.cam.ac.uk/handle/1810/247867

Rights: Attribution 2.0 UK: England & Wales

Licence URL: http://creativecommons.org/licenses/by/2.0/uk/





Autor: Carrara, GuiaSaraiva, NunoParsons, MaddyByrne, BernadetteProle, David L.Taylor, Colin W.Smith, Geoffrey L.

Fuente: https://www.repository.cam.ac.uk/handle/1810/247867



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