The zinc finger domain of IKKγ (NEMO) protein in health and disease
Identifieur interne : 003177 ( Pmc/Checkpoint ); précédent : 003176; suivant : 003178The zinc finger domain of IKKγ (NEMO) protein in health and disease
Auteurs : Amde Selassie ShiferaSource :
- Journal of Cellular and Molecular Medicine [ 1582-1838 ] ; 2010.
Abstract
Inhibitor of κB kinase (IKK) gamma (IKKγ), also known as nuclear factor κB (NF-κB) essential modulator (NEMO), is a component of the IKK complex that is essential for the activation of the NF-κB pathway. The NF-κB pathway plays a major role in the regulation of the expression of genes that are involved in immune response, inflammation, cell adhesion, cell survival and development. As part of the IKK complex, IKKγ plays a regulatory role by linking the complex to upstream signalling molecules. IKKγ contains two coiled-coil regions, a leucine zipper domain and a highly conserved zinc finger domain. Mutations affecting IKKγ have been associated with X-linked hypohidrotic ectodermal dysplasia with immune deficiency (HED-ID), with the majority of these mutations affecting the C-terminal region of the protein where the zinc finger is located. The zinc finger of IKKγ is needed for NF-κB activation in a cell- and stimulus-specific manner. The major mechanism by which the zinc finger plays this role appears to be the recognition of polyubiquitinated upstream signalling intermediates. This assertion reinforces the current notion that ubiquitination plays a major role in mediating protein–protein interactions in the NF-κB signalling pathway. Because the zinc finger domain of IKKγ is very likely involved in mediating interactions with ubiquitinated proteins, investigations that look for upstream activators or inhibitors of the IKK complex that bind to and interact with the zinc finger of IKKγ are required to gain a better insight into the exact roles of this domain and into the pathogenesis of HED-ID.
Url:
DOI: 10.1111/j.1582-4934.2010.01054.x
PubMed: 20345847
PubMed Central: 3823158
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The zinc finger domain of IKKγ (NEMO) protein in health and disease</title><author><name sortKey="Shifera, Amde Selassie" sort="Shifera, Amde Selassie" uniqKey="Shifera A" first="Amde Selassie" last="Shifera">Amde Selassie Shifera</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">20345847</idno><idno type="pmc">3823158</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3823158</idno><idno type="RBID">PMC:3823158</idno><idno type="doi">10.1111/j.1582-4934.2010.01054.x</idno><date when="2010">2010</date><idno type="wicri:Area/Pmc/Corpus">004B09</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">004B09</idno><idno type="wicri:Area/Pmc/Curation">004B08</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">004B08</idno><idno type="wicri:Area/Pmc/Checkpoint">003177</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">003177</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The zinc finger domain of IKKγ (NEMO) protein in health and disease</title><author><name sortKey="Shifera, Amde Selassie" sort="Shifera, Amde Selassie" uniqKey="Shifera A" first="Amde Selassie" last="Shifera">Amde Selassie Shifera</name></author></analytic><series><title level="j">Journal of Cellular and Molecular Medicine</title><idno type="ISSN">1582-1838</idno><idno type="eISSN">1582-4934</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>Inhibitor of κB kinase (IKK) gamma (IKKγ), also known as nuclear factor κB (NF-κB) essential modulator (NEMO), is a component of the IKK complex that is essential for the activation of the NF-κB pathway. The NF-κB pathway plays a major role in the regulation of the expression of genes that are involved in immune response, inflammation, cell adhesion, cell survival and development. As part of the IKK complex, IKKγ plays a regulatory role by linking the complex to upstream signalling molecules. IKKγ contains two coiled-coil regions, a leucine zipper domain and a highly conserved zinc finger domain. Mutations affecting IKKγ have been associated with X-linked hypohidrotic ectodermal dysplasia with immune deficiency (HED-ID), with the majority of these mutations affecting the C-terminal region of the protein where the zinc finger is located. The zinc finger of IKKγ is needed for NF-κB activation in a cell- and stimulus-specific manner. The major mechanism by which the zinc finger plays this role appears to be the recognition of polyubiquitinated upstream signalling intermediates. This assertion reinforces the current notion that ubiquitination plays a major role in mediating protein–protein interactions in the NF-κB signalling pathway. Because the zinc finger domain of IKKγ is very likely involved in mediating interactions with ubiquitinated proteins, investigations that look for upstream activators or inhibitors of the IKK complex that bind to and interact with the zinc finger of IKKγ are required to gain a better insight into the exact roles of this domain and into the pathogenesis of HED-ID.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Yamaoka, S" uniqKey="Yamaoka S">S Yamaoka</name></author><author><name sortKey="Courtois, G" uniqKey="Courtois G">G Courtois</name></author><author><name sortKey="Bessia, C" uniqKey="Bessia C">C Bessia</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rothwarf, Dm" uniqKey="Rothwarf D">DM Rothwarf</name></author><author><name sortKey="Zandi, E" uniqKey="Zandi E">E Zandi</name></author><author><name sortKey="Natoli, G" uniqKey="Natoli G">G 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<front><journal-meta><journal-id journal-id-type="nlm-ta">J Cell Mol Med</journal-id><journal-id journal-id-type="iso-abbrev">J. Cell. Mol. Med</journal-id><journal-id journal-id-type="publisher-id">jcmm</journal-id><journal-title-group><journal-title>Journal of Cellular and Molecular Medicine</journal-title></journal-title-group><issn pub-type="ppub">1582-1838</issn><issn pub-type="epub">1582-4934</issn><publisher><publisher-name>Blackwell Publishing Ltd</publisher-name><publisher-loc>Oxford, UK</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">20345847</article-id><article-id pub-id-type="pmc">3823158</article-id><article-id pub-id-type="doi">10.1111/j.1582-4934.2010.01054.x</article-id><article-categories><subj-group subj-group-type="heading"><subject>Reviews</subject></subj-group></article-categories><title-group><article-title>The zinc finger domain of IKKγ (NEMO) protein in health and disease</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Shifera</surname><given-names>Amde Selassie</given-names></name><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff><institution>Department of Ophthalmology, University of California</institution><addr-line>San Francisco, CA, USA</addr-line></aff></contrib-group><author-notes><corresp id="cor1">*Correspondence to: Amde Selassie SHIFERA, M.D., Ph.D., Department of Ophthalmology, University of California, Box 0730, 10 Koret Way K210, San Francisco, CA 94143, USA. Tel.: 415-476-5430 Fax: 415-476-0336 E-mail: <email>shiferaa@vision.ucsf.edu</email></corresp></author-notes><pub-date pub-type="ppub"><month>10</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>15</day><month>3</month><year>2010</year></pub-date><volume>14</volume><issue>10</issue><fpage>2404</fpage><lpage>2414</lpage><history><date date-type="received"><day>23</day><month>11</month><year>2009</year></date><date date-type="accepted"><day>02</day><month>3</month><year>2010</year></date></history><permissions><copyright-statement>© 2010 The Author Journal compilation © 2010 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd</copyright-statement><copyright-year>2010</copyright-year></permissions><abstract><title>Abstract</title><p>Inhibitor of κB kinase (IKK) gamma (IKKγ), also known as nuclear factor κB (NF-κB) essential modulator (NEMO), is a component of the IKK complex that is essential for the activation of the NF-κB pathway. The NF-κB pathway plays a major role in the regulation of the expression of genes that are involved in immune response, inflammation, cell adhesion, cell survival and development. As part of the IKK complex, IKKγ plays a regulatory role by linking the complex to upstream signalling molecules. IKKγ contains two coiled-coil regions, a leucine zipper domain and a highly conserved zinc finger domain. Mutations affecting IKKγ have been associated with X-linked hypohidrotic ectodermal dysplasia with immune deficiency (HED-ID), with the majority of these mutations affecting the C-terminal region of the protein where the zinc finger is located. The zinc finger of IKKγ is needed for NF-κB activation in a cell- and stimulus-specific manner. The major mechanism by which the zinc finger plays this role appears to be the recognition of polyubiquitinated upstream signalling intermediates. This assertion reinforces the current notion that ubiquitination plays a major role in mediating protein–protein interactions in the NF-κB signalling pathway. Because the zinc finger domain of IKKγ is very likely involved in mediating interactions with ubiquitinated proteins, investigations that look for upstream activators or inhibitors of the IKK complex that bind to and interact with the zinc finger of IKKγ are required to gain a better insight into the exact roles of this domain and into the pathogenesis of HED-ID.</p></abstract><kwd-group><kwd>IKKgamma</kwd><kwd>NEMO</kwd><kwd>zinc finger</kwd><kwd>ubiquitination</kwd><kwd>ectodermal dysplasia</kwd><kwd>hyper IgM syndrome</kwd><kwd>immune deficiency</kwd></kwd-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Shifera, Amde Selassie" sort="Shifera, Amde Selassie" uniqKey="Shifera A" first="Amde Selassie" last="Shifera">Amde Selassie Shifera</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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