Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy
Identifieur interne : 001B58 ( Ncbi/Merge ); précédent : 001B57; suivant : 001B59Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy
Auteurs : Naïma Belgareh-Touzé ; Laetitia Cavellini ; Mickael M. CohenSource :
- Autophagy [ 1554-8627 ] ; 2016.
Abstract
Mitochondria are dynamic organelles that undergo permanent fission and fusion events. These processes play an essential role in maintaining normal cellular function. In the yeast
Url:
DOI: 10.1080/15548627.2016.1252889
PubMed: 27846375
PubMed Central: 5240830
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PMC:5240830Le document en format XML
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<author><name sortKey="Belgareh Touze, Naima" sort="Belgareh Touze, Naima" uniqKey="Belgareh Touze N" first="Naïma" last="Belgareh-Touzé">Naïma Belgareh-Touzé</name>
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<author><name sortKey="Cavellini, Laetitia" sort="Cavellini, Laetitia" uniqKey="Cavellini L" first="Laetitia" last="Cavellini">Laetitia Cavellini</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy</title>
<author><name sortKey="Belgareh Touze, Naima" sort="Belgareh Touze, Naima" uniqKey="Belgareh Touze N" first="Naïma" last="Belgareh-Touzé">Naïma Belgareh-Touzé</name>
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<author><name sortKey="Cavellini, Laetitia" sort="Cavellini, Laetitia" uniqKey="Cavellini L" first="Laetitia" last="Cavellini">Laetitia Cavellini</name>
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<author><name sortKey="Cohen, Mickael M" sort="Cohen, Mickael M" uniqKey="Cohen M" first="Mickael M." last="Cohen">Mickael M. Cohen</name>
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<series><title level="j">Autophagy</title>
<idno type="ISSN">1554-8627</idno>
<idno type="eISSN">1554-8635</idno>
<imprint><date when="2016">2016</date>
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<front><div type="abstract" xml:lang="en"><title>ABSTRACT</title>
<p>Mitochondria are dynamic organelles that undergo permanent fission and fusion events. These processes play an essential role in maintaining normal cellular function. In the yeast <italic>Saccharomyces cerevisiae</italic>
, the endoplasmic reticulum-mitochondrial encounter structure (ERMES) is a marker of sites of mitochondrial division, but it is also involved in a plethora of other mitochondrial functions. However, it remains unclear how these different functions are regulated. We show here that Mdm34 and Mdm12, 2 components of ERMES, are ubiquitinated by the E3 ligase Rsp5. This ubiquitination is not involved in mitochondrial dynamics or in the distribution and turnover of ERMES. Nevertheless, the ubiquitination of Mdm34 and Mdm12 was required for efficient mitophagy. We thus report here the first identification of ubiquitinated substrates participating in yeast mitophagy.</p>
</div>
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</TEI>
<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Autophagy</journal-id>
<journal-id journal-id-type="iso-abbrev">Autophagy</journal-id>
<journal-id journal-id-type="publisher-id">KAUP</journal-id>
<journal-id journal-id-type="publisher-id">kaup20</journal-id>
<journal-title-group><journal-title>Autophagy</journal-title>
</journal-title-group>
<issn pub-type="ppub">1554-8627</issn>
<issn pub-type="epub">1554-8635</issn>
<publisher><publisher-name>Taylor & Francis</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">27846375</article-id>
<article-id pub-id-type="pmc">5240830</article-id>
<article-id pub-id-type="publisher-id">1252889</article-id>
<article-id pub-id-type="doi">10.1080/15548627.2016.1252889</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Basic Research Paper</subject>
</subj-group>
</article-categories>
<title-group><article-title>Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy</article-title>
<alt-title alt-title-type="running-authors">N. BELGAREH-TOUZÉ ET AL.</alt-title>
<alt-title alt-title-type="running-title">AUTOPHAGY</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Belgareh-Touzé</surname>
<given-names>Naïma</given-names>
</name>
<xref ref-type="aff" rid="af0001"></xref>
<xref ref-type="corresp" rid="an0001"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Cavellini</surname>
<given-names>Laetitia</given-names>
</name>
<xref ref-type="aff" rid="af0001"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Cohen</surname>
<given-names>Mickael M.</given-names>
</name>
<xref ref-type="aff" rid="af0001"></xref>
<xref ref-type="corresp" rid="an0001"></xref>
</contrib>
<aff id="af0001"><institution>UMR8226, CNRS/UPMC, Sorbonne Université, Institut de Biologie Physico-Chimique</institution>
, Paris,<country>France</country>
</aff>
</contrib-group>
<author-notes><corresp id="an0001"><bold>CONTACT</bold>
Naïma Belgareh-Touzé <email xlink:href="belgareh@ibpc.fr">belgareh@ibpc.fr</email>
; Mickael M. Cohen <email xlink:href="cohen@ibpc.fr">cohen@ibpc.fr</email>
<institution>UMR8226 CNRS/UPMC Laboratoire: Dynamique membranaire et modifications post-traductionelles</institution>
, <addr-line>13 Rue Pierre et Marie Curie</addr-line>
, 75005 Paris, <country>France</country>
</corresp>
<fn><p>Color versions of one or more of the figures in the article can be found online at <ext-link ext-link-type="uri" xlink:href="http://www.tandfonline.com/kaup">www.tandfonline.com/kaup</ext-link>
.</p>
</fn>
<fn><p>Supplemental data for this article can be accessed on the <ext-link ext-link-type="uri" xlink:href="http://www.tandfonline.com/kaup">publisher's website</ext-link>
.</p>
</fn>
</author-notes>
<pub-date pub-type="collection"><year>2017</year>
</pub-date>
<pub-date pub-type="epub"><day>15</day>
<month>11</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>15</day>
<month>11</month>
<year>2016</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on the . </pmc-comment>
<volume>13</volume>
<issue>1</issue>
<fpage seq="10">114</fpage>
<lpage>132</lpage>
<history><date date-type="received"><day>17</day>
<month>12</month>
<year>2015</year>
</date>
<date date-type="rev-recd"><day>26</day>
<month>9</month>
<year>2016</year>
</date>
<date date-type="accepted"><day>19</day>
<month>10</month>
<year>2016</year>
</date>
</history>
<permissions><pmc-comment> © Naïma Belgareh-Touze, Laetitia Cavellini, and Mickael M. Cohen </pmc-comment>
<copyright-statement>© 2017 The Author(s). Published with license by Taylor & Francis</copyright-statement>
<copyright-year>2017</copyright-year>
<copyright-holder>The Author(s)</copyright-holder>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by-nc/3.0/"><license-p>This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/3.0/">http://creativecommons.org/licenses/by-nc/3.0/</ext-link>
), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.</license-p>
</license>
</permissions>
<self-uri content-type="pdf" xlink:href="kaup-13-01-1252889.pdf"></self-uri>
<abstract><title>ABSTRACT</title>
<p>Mitochondria are dynamic organelles that undergo permanent fission and fusion events. These processes play an essential role in maintaining normal cellular function. In the yeast <italic>Saccharomyces cerevisiae</italic>
, the endoplasmic reticulum-mitochondrial encounter structure (ERMES) is a marker of sites of mitochondrial division, but it is also involved in a plethora of other mitochondrial functions. However, it remains unclear how these different functions are regulated. We show here that Mdm34 and Mdm12, 2 components of ERMES, are ubiquitinated by the E3 ligase Rsp5. This ubiquitination is not involved in mitochondrial dynamics or in the distribution and turnover of ERMES. Nevertheless, the ubiquitination of Mdm34 and Mdm12 was required for efficient mitophagy. We thus report here the first identification of ubiquitinated substrates participating in yeast mitophagy.</p>
</abstract>
<kwd-group kwd-group-type="author"><title>KEYWORDS</title>
<kwd>ER</kwd>
<kwd>ERMES</kwd>
<kwd>Mdm12</kwd>
<kwd>Mdm34</kwd>
<kwd>mitochondria</kwd>
<kwd>mitophagy</kwd>
<kwd>ubiquitin</kwd>
<kwd>Rsp5</kwd>
<kwd><italic>S. cerevisiae</italic>
</kwd>
</kwd-group>
<counts><fig-count count="11"></fig-count>
<table-count count="2"></table-count>
<ref-count count="74"></ref-count>
<page-count count="19"></page-count>
</counts>
</article-meta>
</front>
</pmc>
<affiliations><list></list>
<tree><noCountry><name sortKey="Belgareh Touze, Naima" sort="Belgareh Touze, Naima" uniqKey="Belgareh Touze N" first="Naïma" last="Belgareh-Touzé">Naïma Belgareh-Touzé</name>
<name sortKey="Cavellini, Laetitia" sort="Cavellini, Laetitia" uniqKey="Cavellini L" first="Laetitia" last="Cavellini">Laetitia Cavellini</name>
<name sortKey="Cohen, Mickael M" sort="Cohen, Mickael M" uniqKey="Cohen M" first="Mickael M." last="Cohen">Mickael M. Cohen</name>
</noCountry>
</tree>
</affiliations>
</record>
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