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The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties
The interaction of the anti-apoptotic members of the Bcl-2 family with mitochondria, through their hydrophobic C-terminus, has been proposed to play a crucial role in the execution phase of apoptosis. We report here that a substitution of the C-terminal end of pro-apoptotic bax by that of anti-apopt...
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Published in: | FEBS letters 2000-12, Vol.487 (2), p.161-165 |
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container_title | FEBS letters |
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creator | Oliver, Lisa Priault, Muriel Tremblais, Karine LeCabellec, Marie-Thérèse Meflah, Khaled Manon, Stéphen Vallette, Francois M |
description | The interaction of the anti-apoptotic members of the Bcl-2 family with mitochondria, through their hydrophobic C-terminus, has been proposed to play a crucial role in the execution phase of apoptosis. We report here that a substitution of the C-terminal end of pro-apoptotic bax by that of anti-apoptotic bcl-xL (baxCxL) does not modify its association with mitochondria in human and rat cells or in
Saccharomyces cerevisiae. In addition, while bax sensitizes these cells to apoptotic stimuli, the construct baxCxL does not affect the apoptotic response in transfected cells. These results suggest that the C-terminus of bax plays an important role in apoptosis independently of its membrane addressing/targeting mechanism. |
doi_str_mv | 10.1016/S0014-5793(00)02330-9 |
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Saccharomyces cerevisiae. In addition, while bax sensitizes these cells to apoptotic stimuli, the construct baxCxL does not affect the apoptotic response in transfected cells. These results suggest that the C-terminus of bax plays an important role in apoptosis independently of its membrane addressing/targeting mechanism.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(00)02330-9</identifier><identifier>PMID: 11150501</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Apoptosis ; Apoptosis - drug effects ; Apoptosis - physiology ; Apoptosis - radiation effects ; Bax ; bcl-2-Associated X Protein ; bcl-X Protein ; Cell Membrane - physiology ; Cytosol - physiology ; DEVDase ; Glioma ; Humans ; K562 Cells ; L-Lactate Dehydrogenase - analysis ; Mitochondria - physiology ; Mitochondrion ; Molecular Sequence Data ; Peptide Hydrolases - metabolism ; Proto-Oncogene Proteins - chemistry ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-bcl-2 - chemistry ; Proto-Oncogene Proteins c-bcl-2 - metabolism ; Rats ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - physiology ; Sequence Deletion ; Transfection ; Tumor Cells, Cultured ; Ultraviolet Rays</subject><ispartof>FEBS letters, 2000-12, Vol.487 (2), p.161-165</ispartof><rights>2000 Federation of European Biochemical Societies</rights><rights>FEBS Letters 487 (2000) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4739-38e716dafbf284fd9ca1366d3626b34c835ac3c886774d40d224410e485ccd493</citedby><cites>FETCH-LOGICAL-c4739-38e716dafbf284fd9ca1366d3626b34c835ac3c886774d40d224410e485ccd493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579300023309$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11150501$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oliver, Lisa</creatorcontrib><creatorcontrib>Priault, Muriel</creatorcontrib><creatorcontrib>Tremblais, Karine</creatorcontrib><creatorcontrib>LeCabellec, Marie-Thérèse</creatorcontrib><creatorcontrib>Meflah, Khaled</creatorcontrib><creatorcontrib>Manon, Stéphen</creatorcontrib><creatorcontrib>Vallette, Francois M</creatorcontrib><title>The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The interaction of the anti-apoptotic members of the Bcl-2 family with mitochondria, through their hydrophobic C-terminus, has been proposed to play a crucial role in the execution phase of apoptosis. We report here that a substitution of the C-terminal end of pro-apoptotic bax by that of anti-apoptotic bcl-xL (baxCxL) does not modify its association with mitochondria in human and rat cells or in
Saccharomyces cerevisiae. In addition, while bax sensitizes these cells to apoptotic stimuli, the construct baxCxL does not affect the apoptotic response in transfected cells. These results suggest that the C-terminus of bax plays an important role in apoptosis independently of its membrane addressing/targeting mechanism.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>Apoptosis - radiation effects</subject><subject>Bax</subject><subject>bcl-2-Associated X Protein</subject><subject>bcl-X Protein</subject><subject>Cell Membrane - physiology</subject><subject>Cytosol - physiology</subject><subject>DEVDase</subject><subject>Glioma</subject><subject>Humans</subject><subject>K562 Cells</subject><subject>L-Lactate Dehydrogenase - analysis</subject><subject>Mitochondria - physiology</subject><subject>Mitochondrion</subject><subject>Molecular Sequence Data</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Proto-Oncogene Proteins - chemistry</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-bcl-2 - chemistry</subject><subject>Proto-Oncogene Proteins c-bcl-2 - metabolism</subject><subject>Rats</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Sequence Deletion</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured</subject><subject>Ultraviolet Rays</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqNUcFu1DAQtRCILoVPAPmE6MFgx07inFBZtRRpJQ6Us-XYEzDKxsF2oMtv9Iexsys4wmk0M2_eG72H0HNGXzPKmjefKGWC1G3HX1F6QSvOKekeoA2TLSdcNPIh2vyBnKEnMX6juZese4zOGGM1rSnboPvbr4Dj0sfk0pKcn7AfcMqzLUkQ9m5aYpn0-g73h7zQaW3NSO522HqIePIJ62EAk7BLsXAZGMdl1AGP3ujR_dIrb79kXB_8F53yVYHOwRM9-zn55EzpZgjJQXyKHg16jPDsVM_R5-ur2-0N2X18_2F7uSNGtLwjXELLGquHfqikGGxnNONNY3lTNT0XRvJaG26kbNpWWEFtVQnBKAhZG2NFx8_RyyNvlv6-QExq72J5Xk_gl6jaSmTvKpaB9RFogo8xwKDm4PY6HBSjqqSh1jRUsVpRqtY0VBF4cRJY-j3Yv1cn-zPg5gj46UY4_B-rur56V62bssiZlnHRenukguzYDwdBReNgMmBdyNko690_vv0NGZqvfA</recordid><startdate>20001229</startdate><enddate>20001229</enddate><creator>Oliver, Lisa</creator><creator>Priault, Muriel</creator><creator>Tremblais, Karine</creator><creator>LeCabellec, Marie-Thérèse</creator><creator>Meflah, Khaled</creator><creator>Manon, Stéphen</creator><creator>Vallette, Francois M</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20001229</creationdate><title>The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties</title><author>Oliver, Lisa ; Priault, Muriel ; Tremblais, Karine ; LeCabellec, Marie-Thérèse ; Meflah, Khaled ; Manon, Stéphen ; Vallette, Francois M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4739-38e716dafbf284fd9ca1366d3626b34c835ac3c886774d40d224410e485ccd493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>Apoptosis - radiation effects</topic><topic>Bax</topic><topic>bcl-2-Associated X Protein</topic><topic>bcl-X Protein</topic><topic>Cell Membrane - physiology</topic><topic>Cytosol - physiology</topic><topic>DEVDase</topic><topic>Glioma</topic><topic>Humans</topic><topic>K562 Cells</topic><topic>L-Lactate Dehydrogenase - analysis</topic><topic>Mitochondria - physiology</topic><topic>Mitochondrion</topic><topic>Molecular Sequence Data</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Proto-Oncogene Proteins - chemistry</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-bcl-2 - chemistry</topic><topic>Proto-Oncogene Proteins c-bcl-2 - metabolism</topic><topic>Rats</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Sequence Deletion</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oliver, Lisa</creatorcontrib><creatorcontrib>Priault, Muriel</creatorcontrib><creatorcontrib>Tremblais, Karine</creatorcontrib><creatorcontrib>LeCabellec, Marie-Thérèse</creatorcontrib><creatorcontrib>Meflah, Khaled</creatorcontrib><creatorcontrib>Manon, Stéphen</creatorcontrib><creatorcontrib>Vallette, Francois M</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oliver, Lisa</au><au>Priault, Muriel</au><au>Tremblais, Karine</au><au>LeCabellec, Marie-Thérèse</au><au>Meflah, Khaled</au><au>Manon, Stéphen</au><au>Vallette, Francois M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2000-12-29</date><risdate>2000</risdate><volume>487</volume><issue>2</issue><spage>161</spage><epage>165</epage><pages>161-165</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The interaction of the anti-apoptotic members of the Bcl-2 family with mitochondria, through their hydrophobic C-terminus, has been proposed to play a crucial role in the execution phase of apoptosis. We report here that a substitution of the C-terminal end of pro-apoptotic bax by that of anti-apoptotic bcl-xL (baxCxL) does not modify its association with mitochondria in human and rat cells or in
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subjects | Amino Acid Sequence Animals Apoptosis Apoptosis - drug effects Apoptosis - physiology Apoptosis - radiation effects Bax bcl-2-Associated X Protein bcl-X Protein Cell Membrane - physiology Cytosol - physiology DEVDase Glioma Humans K562 Cells L-Lactate Dehydrogenase - analysis Mitochondria - physiology Mitochondrion Molecular Sequence Data Peptide Hydrolases - metabolism Proto-Oncogene Proteins - chemistry Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-bcl-2 - chemistry Proto-Oncogene Proteins c-bcl-2 - metabolism Rats Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - physiology Sequence Deletion Transfection Tumor Cells, Cultured Ultraviolet Rays |
title | The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties |
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