期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 18, 页码 11785-11801出版社
ELSEVIER
DOI: 10.1074/jbc.M115.637306
关键词
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资金
- United Kingdom Medical Research Council
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust
- BBSRC [BB/L000075/1] Funding Source: UKRI
- MRC [G0900224] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L000075/1] Funding Source: researchfish
- Medical Research Council [G0900224] Funding Source: researchfish
- Wellcome Trust [101844/Z/13/Z] Funding Source: researchfish
- Wellcome Trust [101844/Z/13/Z] Funding Source: Wellcome Trust
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.
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