In this section
@article{Carrara:2015:10.1074/jbc.M115.637306,
author = {Carrara, G and Saraiva, N and Parsons, M and Byrne, B and Prole, DL and Taylor, CW and Smith, GL},
doi = {10.1074/jbc.M115.637306},
journal = {Journal of Biological Chemistry},
pages = {11785--11801},
title = {Golgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration},
url = {http://dx.doi.org/10.1074/jbc.M115.637306},
volume = {290},
year = {2015}
}
TY - JOUR
AB - 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.Background: GAAPs regulate intracellular Ca2+ fluxes, cell migration, and apoptosis.Results: GAAP forms a cation-selective channel, and residues involved in its ion-conducting properties were identified.Conclusion: Mutations within the pore demonstrate that GAAP effects on apoptosis and migration are separable.Significance: Characterization of the pore region of GAAP provides insight into the mechanism of action of this novel and highly conserved ion channel.
AU - Carrara,G
AU - Saraiva,N
AU - Parsons,M
AU - Byrne,B
AU - Prole,DL
AU - Taylor,CW
AU - Smith,GL
DO - 10.1074/jbc.M115.637306
EP - 11801
PY - 2015///
SN - 0021-9258
SP - 11785
TI - Golgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration
T2 - Journal of Biological Chemistry
UR - http://dx.doi.org/10.1074/jbc.M115.637306
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000353719400050&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://www.sciencedirect.com/science/article/pii/S0021925820570130?via%3Dihub
UR - http://hdl.handle.net/10044/1/94014
VL - 290
ER -
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