Differential retrotranslocation of mitochondrial Bax and Bak
The Bcl‐2 proteins Bax and Bak can permeabilize the outer mitochondrial membrane and commit cells to apoptosis. Pro‐survival Bcl‐2 proteins control Bax by constant retrotranslocation into the cytosol of healthy cells. The stabilization of cytosolic Bax raises the question whether the functionally re...
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| creator | Todt, Franziska Cakir, Zeynep Reichenbach, Frank Emschermann, Frederic Lauterwasser, Joachim Kaiser, Andrea Ichim, Gabriel Tait, Stephen WG Frank, Stephan Langer, Harald F Edlich, Frank |
| description | The Bcl‐2 proteins Bax and Bak can permeabilize the outer mitochondrial membrane and commit cells to apoptosis. Pro‐survival Bcl‐2 proteins control Bax by constant retrotranslocation into the cytosol of healthy cells. The stabilization of cytosolic Bax raises the question whether the functionally redundant but largely mitochondrial Bak shares this level of regulation. Here we report that Bak is retrotranslocated from the mitochondria by pro‐survival Bcl‐2 proteins. Bak is present in the cytosol of human cells and tissues, but low shuttling rates cause predominant mitochondrial Bak localization. Interchanging the membrane anchors of Bax and Bak reverses their subcellular localization compared to the wild‐type proteins. Strikingly, the reduction of Bax shuttling to the level of Bak retrotranslocation results in full Bax toxicity even in absence of apoptosis induction. Thus, fast Bax retrotranslocation is required to protect cells from commitment to programmed death.
Synopsis
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor.
The pro‐apoptotic Bcl‐2 protein Bak is retrotranslocated from the mitochondria into the cytosol dependent on pro‐survival Bcl‐2 proteins.
Bax and Bak retrotranslocate at different rates by the same retrotranslocation process.
Rapid Bax shuttling protects cells from apoptosis in the presence or absence of apoptotic stimuli.
The hydrophobicity of the membrane anchor determines shuttling and localization of Bax and Bak.
Graphical Abstract
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor. |
| doi_str_mv | 10.15252/embj.201488806 |
| format | Article |
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Synopsis
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor.
The pro‐apoptotic Bcl‐2 protein Bak is retrotranslocated from the mitochondria into the cytosol dependent on pro‐survival Bcl‐2 proteins.
Bax and Bak retrotranslocate at different rates by the same retrotranslocation process.
Rapid Bax shuttling protects cells from apoptosis in the presence or absence of apoptotic stimuli.
The hydrophobicity of the membrane anchor determines shuttling and localization of Bax and Bak.
Graphical Abstract
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.15252/embj.201488806</identifier><identifier>PMID: 25378477</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Blackwell Publishing Ltd</publisher><subject>Apoptosis ; Apoptosis - physiology ; bcl-2 Homologous Antagonist-Killer Protein - genetics ; bcl-2 Homologous Antagonist-Killer Protein - metabolism ; Bcl-2 proteins ; bcl-2-Associated X Protein - genetics ; bcl-2-Associated X Protein - metabolism ; Cell Line ; Cytosol - metabolism ; EMBO07 ; Humans ; membrane association ; Membranes ; Mitochondria - genetics ; Mitochondria - metabolism ; Mitochondrial DNA ; Mitochondrial Proteins - genetics ; Mitochondrial Proteins - metabolism ; Protein Transport - physiology ; Proteins ; tail anchor</subject><ispartof>The EMBO journal, 2015-01, Vol.34 (1), p.67-80</ispartof><rights>The Authors 2014</rights><rights>2014 The Authors</rights><rights>2014 The Authors.</rights><rights>2015 EMBO</rights><rights>2014 The Authors 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6176-cfe8545eb8d58fd6856bd1b9305b047717425ccad5a23fc823c776e1a776ea9c3</citedby><cites>FETCH-LOGICAL-c6176-cfe8545eb8d58fd6856bd1b9305b047717425ccad5a23fc823c776e1a776ea9c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4291481/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4291481/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,41096,42165,45550,45551,46384,46808,51551,53766,53768</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.15252/embj.201488806$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25378477$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Todt, Franziska</creatorcontrib><creatorcontrib>Cakir, Zeynep</creatorcontrib><creatorcontrib>Reichenbach, Frank</creatorcontrib><creatorcontrib>Emschermann, Frederic</creatorcontrib><creatorcontrib>Lauterwasser, Joachim</creatorcontrib><creatorcontrib>Kaiser, Andrea</creatorcontrib><creatorcontrib>Ichim, Gabriel</creatorcontrib><creatorcontrib>Tait, Stephen WG</creatorcontrib><creatorcontrib>Frank, Stephan</creatorcontrib><creatorcontrib>Langer, Harald F</creatorcontrib><creatorcontrib>Edlich, Frank</creatorcontrib><title>Differential retrotranslocation of mitochondrial Bax and Bak</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>The Bcl‐2 proteins Bax and Bak can permeabilize the outer mitochondrial membrane and commit cells to apoptosis. Pro‐survival Bcl‐2 proteins control Bax by constant retrotranslocation into the cytosol of healthy cells. The stabilization of cytosolic Bax raises the question whether the functionally redundant but largely mitochondrial Bak shares this level of regulation. Here we report that Bak is retrotranslocated from the mitochondria by pro‐survival Bcl‐2 proteins. Bak is present in the cytosol of human cells and tissues, but low shuttling rates cause predominant mitochondrial Bak localization. Interchanging the membrane anchors of Bax and Bak reverses their subcellular localization compared to the wild‐type proteins. Strikingly, the reduction of Bax shuttling to the level of Bak retrotranslocation results in full Bax toxicity even in absence of apoptosis induction. Thus, fast Bax retrotranslocation is required to protect cells from commitment to programmed death.
Synopsis
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor.
The pro‐apoptotic Bcl‐2 protein Bak is retrotranslocated from the mitochondria into the cytosol dependent on pro‐survival Bcl‐2 proteins.
Bax and Bak retrotranslocate at different rates by the same retrotranslocation process.
Rapid Bax shuttling protects cells from apoptosis in the presence or absence of apoptotic stimuli.
The hydrophobicity of the membrane anchor determines shuttling and localization of Bax and Bak.
Graphical Abstract
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor.</description><subject>Apoptosis</subject><subject>Apoptosis - physiology</subject><subject>bcl-2 Homologous Antagonist-Killer Protein - genetics</subject><subject>bcl-2 Homologous Antagonist-Killer Protein - metabolism</subject><subject>Bcl-2 proteins</subject><subject>bcl-2-Associated X Protein - genetics</subject><subject>bcl-2-Associated X Protein - metabolism</subject><subject>Cell Line</subject><subject>Cytosol - metabolism</subject><subject>EMBO07</subject><subject>Humans</subject><subject>membrane association</subject><subject>Membranes</subject><subject>Mitochondria - genetics</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial DNA</subject><subject>Mitochondrial Proteins - genetics</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Protein Transport - physiology</subject><subject>Proteins</subject><subject>tail anchor</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkElPwzAQhS0EomU5c0OVOKfYTrwUISQobdlBLOJoOY4DLmlc7BTov8clUJUD4jJzmO-9eXoAbCHYRgQTvKtH6bCNIUo455AugSZKKIwwZGQZNCGmKEoQ7zTAmvdDCCHhDK2CBiYx4wljTbB_bPJcO11WRhYtpytnKydLX1glK2PLls1bI1NZ9WzLzM2YI_nRkmUW9ssGWMll4fXm914HD_3effckurgenHYPLyJFEaORyjUnCdEpzwjPM8oJTTOUdmJIUhhSIJZgopTMiMRxrjiOFWNUIzmbsqPidXBQ-44n6UhnKqR1shBjZ0bSTYWVRvy-lOZZPNk3keBOaAYFg51vA2dfJ9pXYmgnrgyZBaJJQAiLcaB2a0o5673T-fwDguKrbjGrW8zrDortxWBz_qffAOzVwLsp9PQ_P9G7PDpbdIe12Add-aTdQuo_A0W1xPhKf8z_SfciKIsZEY9XA9G9QXeD2_5AnMefEwCsYA</recordid><startdate>20150102</startdate><enddate>20150102</enddate><creator>Todt, Franziska</creator><creator>Cakir, Zeynep</creator><creator>Reichenbach, Frank</creator><creator>Emschermann, Frederic</creator><creator>Lauterwasser, Joachim</creator><creator>Kaiser, Andrea</creator><creator>Ichim, Gabriel</creator><creator>Tait, Stephen WG</creator><creator>Frank, Stephan</creator><creator>Langer, Harald F</creator><creator>Edlich, Frank</creator><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group UK</general><general>BlackWell Publishing Ltd</general><scope>BSCLL</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20150102</creationdate><title>Differential retrotranslocation of mitochondrial Bax and Bak</title><author>Todt, Franziska ; 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Pro‐survival Bcl‐2 proteins control Bax by constant retrotranslocation into the cytosol of healthy cells. The stabilization of cytosolic Bax raises the question whether the functionally redundant but largely mitochondrial Bak shares this level of regulation. Here we report that Bak is retrotranslocated from the mitochondria by pro‐survival Bcl‐2 proteins. Bak is present in the cytosol of human cells and tissues, but low shuttling rates cause predominant mitochondrial Bak localization. Interchanging the membrane anchors of Bax and Bak reverses their subcellular localization compared to the wild‐type proteins. Strikingly, the reduction of Bax shuttling to the level of Bak retrotranslocation results in full Bax toxicity even in absence of apoptosis induction. Thus, fast Bax retrotranslocation is required to protect cells from commitment to programmed death.
Synopsis
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor.
The pro‐apoptotic Bcl‐2 protein Bak is retrotranslocated from the mitochondria into the cytosol dependent on pro‐survival Bcl‐2 proteins.
Bax and Bak retrotranslocate at different rates by the same retrotranslocation process.
Rapid Bax shuttling protects cells from apoptosis in the presence or absence of apoptotic stimuli.
The hydrophobicity of the membrane anchor determines shuttling and localization of Bax and Bak.
Graphical Abstract
Pro‐apoptotic proteins Bax and Bak kill cells by permeabilizing the outer mitochondrial membrane. Mitochondrial localization and thus apoptosis induction by both proteins is controlled by their retrotranslocation dynamics governed by the hydrophobicity of the C‐terminal membrane anchor.</abstract><cop>London</cop><pub>Blackwell Publishing Ltd</pub><pmid>25378477</pmid><doi>10.15252/embj.201488806</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Apoptosis Apoptosis - physiology bcl-2 Homologous Antagonist-Killer Protein - genetics bcl-2 Homologous Antagonist-Killer Protein - metabolism Bcl-2 proteins bcl-2-Associated X Protein - genetics bcl-2-Associated X Protein - metabolism Cell Line Cytosol - metabolism EMBO07 Humans membrane association Membranes Mitochondria - genetics Mitochondria - metabolism Mitochondrial DNA Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Protein Transport - physiology Proteins tail anchor |
| title | Differential retrotranslocation of mitochondrial Bax and Bak |
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