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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The PARL family of mitochondrial rhomboid proteases</title><author><name sortKey="Hill, R Blake" sort="Hill, R Blake" uniqKey="Hill R" first="R. Blake" last="Hill">R. Blake Hill</name><affiliation><nlm:aff id="A1"> Departments of Biology and Chemistry, Johns Hopkins University, Baltimore, MD, USA</nlm:aff></affiliation></author><author><name sortKey="Pellegrini, Luca" sort="Pellegrini, Luca" uniqKey="Pellegrini L" first="Luca" last="Pellegrini">Luca Pellegrini</name><affiliation><nlm:aff id="A2"> Department of Molecular Biology, Medical Biochemistry and Pathology, Faculty of Medicine, Université Laval, Quebec, Canada</nlm:aff></affiliation><affiliation><nlm:aff id="A3"> Mitochondria Biology Laboratory, CRULRG, Université Laval, Quebec, Canada</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">20045481</idno><idno type="pmc">2908206</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2908206</idno><idno type="RBID">PMC:2908206</idno><idno type="doi">10.1016/j.semcdb.2009.12.011</idno><date when="2010">2010</date><idno type="wicri:Area/Pmc/Corpus">000456</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000456</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The PARL family of mitochondrial rhomboid proteases</title><author><name sortKey="Hill, R Blake" sort="Hill, R Blake" uniqKey="Hill R" first="R. Blake" last="Hill">R. Blake Hill</name><affiliation><nlm:aff id="A1"> Departments of Biology and Chemistry, Johns Hopkins University, Baltimore, MD, USA</nlm:aff></affiliation></author><author><name sortKey="Pellegrini, Luca" sort="Pellegrini, Luca" uniqKey="Pellegrini L" first="Luca" last="Pellegrini">Luca Pellegrini</name><affiliation><nlm:aff id="A2"> Department of Molecular Biology, Medical Biochemistry and Pathology, Faculty of Medicine, Université Laval, Quebec, Canada</nlm:aff></affiliation><affiliation><nlm:aff id="A3"> Mitochondria Biology Laboratory, CRULRG, Université Laval, Quebec, Canada</nlm:aff></affiliation></author></analytic><series><title level="j">Seminars in cell & developmental biology</title><idno type="ISSN">1084-9521</idno><idno type="eISSN">1096-3634</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">Rhomboids are an ancient and conserved family of intramembrane-cleaving proteases, a small group of proteolytic enzymes capable of hydrolyzing a peptide bond within a transmembrane helix that anchors a substrate protein to the membrane. Mitochondrial rhomboids evolved in eukaryotes to coordinate a critical aspect of cell biology, the regulation of mitochondrial membranes dynamics. This function appears to have required the emergence of a structural feature that is unique among all other rhomboids: an additional transmembrane helix (TMH) positioned at the N-terminus of six TMHs that form the core proteolytic domain of all prokaryotic and eukaryotic rhomboids. This “1+6” structure, which is shared only among mitochondrial rhomboids, defines a subfamily of rhomboids with the prototypical family member being mammalian Parl. Here, we present the findings that in eleven years have elevated mitochondrial rhomboids as the gatekeepers of mitochondrial dynamics and apoptosis; further, we discuss the aspects of their biology that are bound to introduce new paradigm shifts in our understanding of how the organelle uses this unique type of protease to govern stress, signaling to the nucleus, and other key mitochondrial activities in health and disease.</p></div></front></TEI><pmc article-type="research-article" xml:lang="EN"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">9607332</journal-id><journal-id journal-id-type="pubmed-jr-id">20707</journal-id><journal-id journal-id-type="nlm-ta">Semin Cell Dev Biol</journal-id><journal-title>Seminars in cell & developmental biology</journal-title><issn pub-type="ppub">1084-9521</issn><issn pub-type="epub">1096-3634</issn></journal-meta><article-meta><article-id pub-id-type="pmid">20045481</article-id><article-id pub-id-type="pmc">2908206</article-id><article-id pub-id-type="doi">10.1016/j.semcdb.2009.12.011</article-id><article-id pub-id-type="manuscript">NIHMS168505</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>The PARL family of mitochondrial rhomboid proteases</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Hill</surname><given-names>R. Blake</given-names></name><xref rid="A1" ref-type="aff">1</xref><xref rid="FN1" ref-type="author-notes">*</xref></contrib><contrib contrib-type="author"><name><surname>Pellegrini</surname><given-names>Luca</given-names></name><xref rid="A2" ref-type="aff">2</xref><xref rid="A3" ref-type="aff">3</xref><xref rid="FN1" ref-type="author-notes">*</xref></contrib></contrib-group><aff id="A1"><label>1</label> Departments of Biology and Chemistry, Johns Hopkins University, Baltimore, MD, USA</aff><aff id="A2"><label>2</label> Department of Molecular Biology, Medical Biochemistry and Pathology, Faculty of Medicine, Université Laval, Quebec, Canada</aff><aff id="A3"><label>3</label> Mitochondria Biology Laboratory, CRULRG, Université Laval, Quebec, Canada</aff><author-notes><corresp id="FN1"><label>*</label> Corresponding Authors: <email>hill@jhu.edu</email> (R.B. Hill), <email>luca.pellegrini@crulrg.ulaval.ca</email> (L. Pellegrini)</corresp></author-notes><pub-date pub-type="nihms-submitted"><day>20</day><month>2</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>4</day><month>1</month><year>2010</year></pub-date><pub-date pub-type="ppub"><month>8</month><year>2010</year></pub-date><pub-date pub-type="pmc-release"><day>1</day><month>8</month><year>2011</year></pub-date><volume>21</volume><issue>6</issue><fpage>582</fpage><lpage>592</lpage><abstract><p id="P1">Rhomboids are an ancient and conserved family of intramembrane-cleaving proteases, a small group of proteolytic enzymes capable of hydrolyzing a peptide bond within a transmembrane helix that anchors a substrate protein to the membrane. Mitochondrial rhomboids evolved in eukaryotes to coordinate a critical aspect of cell biology, the regulation of mitochondrial membranes dynamics. This function appears to have required the emergence of a structural feature that is unique among all other rhomboids: an additional transmembrane helix (TMH) positioned at the N-terminus of six TMHs that form the core proteolytic domain of all prokaryotic and eukaryotic rhomboids. This “1+6” structure, which is shared only among mitochondrial rhomboids, defines a subfamily of rhomboids with the prototypical family member being mammalian Parl. Here, we present the findings that in eleven years have elevated mitochondrial rhomboids as the gatekeepers of mitochondrial dynamics and apoptosis; further, we discuss the aspects of their biology that are bound to introduce new paradigm shifts in our understanding of how the organelle uses this unique type of protease to govern stress, signaling to the nucleus, and other key mitochondrial activities in health and disease.</p></abstract><kwd-group><kwd>Mitochondria</kwd><kwd>rhomboids</kwd><kwd>serine protease</kwd><kwd>regulated intramembrane proteolysis</kwd><kwd>catalytic dyad</kwd><kwd>membrane dynamics</kwd><kwd>apoptosis</kwd><kwd>Parl</kwd><kwd>Opa1</kwd><kwd>Hax1</kwd><kwd>Omi</kwd><kwd>Htr2A</kwd><kwd>Mgm1</kwd><kwd>mitochondrial stress</kwd><kwd>retrograde signaling</kwd><kwd>neurodegenerative disease</kwd><kwd>Parkinson's disease</kwd><kwd>cancer</kwd></kwd-group><contract-num rid="GM1">R01 GM067180-05S1
||GM</contract-num><contract-num rid="GM1">R01 GM067180-05
||GM</contract-num><contract-sponsor id="GM1">National Institute of General Medical Sciences : NIGMS</contract-sponsor></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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