<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Vafiadaki, E.</style></author><author><style face="normal" font="default" size="100%">Arvanitis, DA</style></author><author><style face="normal" font="default" size="100%">Pagakis, S. N.</style></author><author><style face="normal" font="default" size="100%">Papalouka, V.</style></author><author><style face="normal" font="default" size="100%">Sanoudou, D.</style></author><author><style face="normal" font="default" size="100%">Kontrogianni-Konstantopoulos, A.</style></author><author><style face="normal" font="default" size="100%">Kranias, EG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Biol CellMol Biol CellMol Biol Cell</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Molecular biology of the cell</style></alt-title><short-title><style face="normal" font="default" size="100%">Molecular biology of the cellMolecular biology of the cell</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Cell Survival</style></keyword><keyword><style  face="normal" font="default" size="100%">Adaptor Proteins, Signal Transducing</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium-Binding Proteins/genetics/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Inhibitors/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen Peroxide/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidants/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Interaction Mapping</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteins/genetics/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarcoplasmic Reticulum Calcium-Transporting ATPases/genetics/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Thapsigargin/metabolism</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Jan</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">306-18</style></pages><isbn><style face="normal" font="default" size="100%">1939-4586 (Electronic)1059-1524 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Cardiac contractility is regulated through the activity of various key Ca(2+)-handling proteins. The sarco(endo)plasmic reticulum (SR) Ca(2+) transport ATPase (SERCA2a) and its inhibitor phospholamban (PLN) control the uptake of Ca(2+) by SR membranes during relaxation. Recently, the antiapoptotic HS-1-associated protein X-1 (HAX-1) was identified as a binding partner of PLN, and this interaction was postulated to regulate cell apoptosis. In the current study, we determined that HAX-1 can also bind to SERCA2. Deletion mapping analysis demonstrated that amino acid residues 575-594 of SERCA2's nucleotide binding domain are required for its interaction with the C-terminal domain of HAX-1, containing amino acids 203-245. In transiently cotransfected human embryonic kidney 293 cells, recombinant SERCA2 was specifically targeted to the ER, whereas HAX-1 selectively concentrated at mitochondria. On triple transfections with PLN, however, HAX-1 massively translocated to the ER membranes, where it codistributed with PLN and SERCA2. Overexpression of SERCA2 abrogated the protective effects of HAX-1 on cell survival, after hypoxia/reoxygenation or thapsigargin treatment. Importantly, HAX-1 overexpression was associated with down-regulation of SERCA2 expression levels, resulting in significant reduction of apparent ER Ca(2+) levels. These findings suggest that HAX-1 may promote cell survival through modulation of SERCA2 protein levels and thus ER Ca(2+) stores.</style></abstract><accession-num><style face="normal" font="default" size="100%">18971376</style></accession-num><notes><style face="normal" font="default" size="100%">Vafiadaki, ElizabethArvanitis, Demetrios APagakis, Stamatis NPapalouka, VasilikiSanoudou, DespinaKontrogianni-Konstantopoulos, AikateriniKranias, Evangelia GengHL26057/HL/NHLBI NIH HHS/R37 HL026057/HL/NHLBI NIH HHS/HL77101/HL/NHLBI NIH HHS/R01 HL026057/HL/NHLBI NIH HHS/HL64018/HL/NHLBI NIH HHS/R01 HL064018/HL/NHLBI NIH HHS/P50 HL077101/HL/NHLBI NIH HHS/Research Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov't2008/10/31 09:00Mol Biol Cell. 2009 Jan;20(1):306-18. doi: 10.1091/mbc.e08-06-0587. Epub 2008 Oct 29.</style></notes><custom2><style face="normal" font="default" size="100%">2613088</style></custom2><auth-address><style face="normal" font="default" size="100%">Molecular Biology Division, Biomedical Research Foundation, Academy of Athens, Greece.</style></auth-address></record></records></xml>