LymphedemaV1, Pmc, Corpus, bibRecord, 000282

Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders*

Identifieur interne : 000282 ( Pmc/Corpus ); précédent : 000281; suivant : 000283

Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders*

Auteurs : Norihito Shibata ; Nobumichi Ohoka ; Yusuke Sugaki ; Chiaki Onodera ; Mizuho Inoue ; Yoshiyuki Sakuraba ; Daisuke Takakura ; Noritaka Hashii ; Nana Kawasaki ; Yoichi Gondo ; Mikihiko Naito

Source :

The Journal of Biological Chemistry [ 0021-9258 ] ; 2015.

RBID : PMC:4653699

Abstract

Background: 20 read-through mutations that produce C-terminally extended proteins are related to human hereditary disorders.

Results: The C-terminal extended proteins of mouse cFLIP-L (cellular FLICE-like apoptosisinhibitory protein) and human PNPO (pyridoxamine 5-phosphate oxidase) and HSD3B2 (3-hydroxysteroid dehydrogenase type II) are ubiquitylated and degraded, involving an E3 ligase, TRIM21, for cFLIP-L and PNPO degradation.

Conclusion: Read-through mutant cFLIP-L, PNPO, and HSD3B2 are degraded by the ubiquitin-proteasome system.

Significance: Degradation of read-through mutant proteins may cause hereditary disorders.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4653699

DOI: 10.1074/jbc.M115.670901
PubMed: 26442586
PubMed Central: 4653699

Links to Exploration step

PMC:4653699

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Shibata, Norihito" sort="Shibata, Norihito" uniqKey="Shibata N" first="Norihito" last="Shibata">Norihito Shibata</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Ohoka, Nobumichi" sort="Ohoka, Nobumichi" uniqKey="Ohoka N" first="Nobumichi" last="Ohoka">Nobumichi Ohoka</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Sugaki, Yusuke" sort="Sugaki, Yusuke" uniqKey="Sugaki Y" first="Yusuke" last="Sugaki">Yusuke Sugaki</name>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Onodera, Chiaki" sort="Onodera, Chiaki" uniqKey="Onodera C" first="Chiaki" last="Onodera">Chiaki Onodera</name>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Inoue, Mizuho" sort="Inoue, Mizuho" uniqKey="Inoue M" first="Mizuho" last="Inoue">Mizuho Inoue</name>
<affiliation><nlm:aff id="aff4"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Sakuraba, Yoshiyuki" sort="Sakuraba, Yoshiyuki" uniqKey="Sakuraba Y" first="Yoshiyuki" last="Sakuraba">Yoshiyuki Sakuraba</name>
<affiliation><nlm:aff id="aff5"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Takakura, Daisuke" sort="Takakura, Daisuke" uniqKey="Takakura D" first="Daisuke" last="Takakura">Daisuke Takakura</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hashii, Noritaka" sort="Hashii, Noritaka" uniqKey="Hashii N" first="Noritaka" last="Hashii">Noritaka Hashii</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kawasaki, Nana" sort="Kawasaki, Nana" uniqKey="Kawasaki N" first="Nana" last="Kawasaki">Nana Kawasaki</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Gondo, Yoichi" sort="Gondo, Yoichi" uniqKey="Gondo Y" first="Yoichi" last="Gondo">Yoichi Gondo</name>
<affiliation><nlm:aff id="aff5"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Naito, Mikihiko" sort="Naito, Mikihiko" uniqKey="Naito M" first="Mikihiko" last="Naito">Mikihiko Naito</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">26442586</idno>
<idno type="pmc">4653699</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4653699</idno>
<idno type="RBID">PMC:4653699</idno>
<idno type="doi">10.1074/jbc.M115.670901</idno>
<date when="2015">2015</date>
<idno type="wicri:Area/Pmc/Corpus">000282</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000282</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Shibata, Norihito" sort="Shibata, Norihito" uniqKey="Shibata N" first="Norihito" last="Shibata">Norihito Shibata</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Ohoka, Nobumichi" sort="Ohoka, Nobumichi" uniqKey="Ohoka N" first="Nobumichi" last="Ohoka">Nobumichi Ohoka</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Sugaki, Yusuke" sort="Sugaki, Yusuke" uniqKey="Sugaki Y" first="Yusuke" last="Sugaki">Yusuke Sugaki</name>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Onodera, Chiaki" sort="Onodera, Chiaki" uniqKey="Onodera C" first="Chiaki" last="Onodera">Chiaki Onodera</name>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Inoue, Mizuho" sort="Inoue, Mizuho" uniqKey="Inoue M" first="Mizuho" last="Inoue">Mizuho Inoue</name>
<affiliation><nlm:aff id="aff4"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Sakuraba, Yoshiyuki" sort="Sakuraba, Yoshiyuki" uniqKey="Sakuraba Y" first="Yoshiyuki" last="Sakuraba">Yoshiyuki Sakuraba</name>
<affiliation><nlm:aff id="aff5"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Takakura, Daisuke" sort="Takakura, Daisuke" uniqKey="Takakura D" first="Daisuke" last="Takakura">Daisuke Takakura</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hashii, Noritaka" sort="Hashii, Noritaka" uniqKey="Hashii N" first="Noritaka" last="Hashii">Noritaka Hashii</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kawasaki, Nana" sort="Kawasaki, Nana" uniqKey="Kawasaki N" first="Nana" last="Kawasaki">Nana Kawasaki</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Gondo, Yoichi" sort="Gondo, Yoichi" uniqKey="Gondo Y" first="Yoichi" last="Gondo">Yoichi Gondo</name>
<affiliation><nlm:aff id="aff5"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Naito, Mikihiko" sort="Naito, Mikihiko" uniqKey="Naito M" first="Mikihiko" last="Naito">Mikihiko Naito</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
<imprint><date when="2015">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
 20 read-through mutations that produce C-terminally extended proteins are related to human hereditary disorders.</p>
<p><bold>Results:</bold>
 The C-terminal extended proteins of mouse cFLIP-L (cellular FLICE-like apoptosisinhibitory protein) and human PNPO (pyridoxamine 5-phosphate oxidase) and HSD3B2 (3-hydroxysteroid dehydrogenase type II) are ubiquitylated and degraded, involving an E3 ligase, TRIM21, for cFLIP-L and PNPO degradation.</p>
<p><bold>Conclusion:</bold>
 Read-through mutant cFLIP-L, PNPO, and HSD3B2 are degraded by the ubiquitin-proteasome system.</p>
<p><bold>Significance:</bold>
 Degradation of read-through mutant proteins may cause hereditary disorders.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
  <front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id>
<journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id>
<journal-id journal-id-type="hwp">jbc</journal-id>
<journal-id journal-id-type="pmc">jbc</journal-id>
<journal-id journal-id-type="publisher-id">JBC</journal-id>
<journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9258</issn>
<issn pub-type="epub">1083-351X</issn>
<publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name>
<publisher-loc>11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A.</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">26442586</article-id>
<article-id pub-id-type="pmc">4653699</article-id>
<article-id pub-id-type="publisher-id">M115.670901</article-id>
<article-id pub-id-type="doi">10.1074/jbc.M115.670901</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Molecular Bases of Disease</subject>
</subj-group>
</article-categories>
<title-group><article-title>Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</article-title>
<alt-title alt-title-type="short">Degradation of Read-through Mutant Proteins</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Shibata</surname>
<given-names>Norihito</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ohoka</surname>
<given-names>Nobumichi</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Sugaki</surname>
<given-names>Yusuke</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Onodera</surname>
<given-names>Chiaki</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Inoue</surname>
<given-names>Mizuho</given-names>
</name>
<xref ref-type="aff" rid="aff4"><sup>¶</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Sakuraba</surname>
<given-names>Yoshiyuki</given-names>
</name>
<xref ref-type="aff" rid="aff5"><sup>‖</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Takakura</surname>
<given-names>Daisuke</given-names>
</name>
<xref ref-type="aff" rid="aff2">**</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Hashii</surname>
<given-names>Noritaka</given-names>
</name>
<xref ref-type="aff" rid="aff2">**</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kawasaki</surname>
<given-names>Nana</given-names>
</name>
<xref ref-type="aff" rid="aff2">**</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Gondo</surname>
<given-names>Yoichi</given-names>
</name>
<xref ref-type="aff" rid="aff5"><sup>‖</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Naito</surname>
<given-names>Mikihiko</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="corresp" rid="cor1"><sup>1</sup>
</xref>
</contrib>
<aff id="aff1">From the<label>‡</label>
Division of Molecular Target and Gene Therapy Products and</aff>
<aff id="aff2">the<label>**</label>
Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, Setagaya-ku, Tokyo 158-8501, Japan,</aff>
<aff id="aff3">the<label>§</label>
Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, Chiba 277-8561, Japan,</aff>
<aff id="aff4">the<label>¶</label>
Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan,</aff>
<aff id="aff5">the<label>‖</label>
Mutagenesis and Genomics Team, RIKEN BioResource Center, Tsukuba, Ibaraki 305-0074, Japan</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>1</label>
 To whom correspondence should be addressed: <addr-line>Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan.</addr-line>
 Tel.: <phone>81-3-3700-9428</phone>
; Fax: <fax>81-3-3707-6950</fax>
; E-mail: <email>miki-naito@nihs.go.jp</email>
.</corresp>
</author-notes>
<pub-date pub-type="ppub"><day>20</day>
<month>11</month>
<year>2015</year>
</pub-date>
<pub-date pub-type="epub"><day>6</day>
<month>10</month>
<year>2015</year>
</pub-date>
<volume>290</volume>
<issue>47</issue>
<fpage>28428</fpage>
<lpage>28437</lpage>
<history><date date-type="received"><day>8</day>
<month>6</month>
<year>2015</year>
</date>
<date date-type="rev-recd"><day>2</day>
<month>10</month>
<year>2015</year>
</date>
</history>
<permissions><copyright-statement>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement>
<copyright-year>2015</copyright-year>
<copyright-holder>The American Society for Biochemistry and Molecular Biology, Inc.</copyright-holder>
</permissions>
<self-uri content-type="pdf" xlink:href="zbc04715028428.pdf"></self-uri>
<abstract abstract-type="teaser"><p><bold>Background:</bold>
 20 read-through mutations that produce C-terminally extended proteins are related to human hereditary disorders.</p>
<p><bold>Results:</bold>
 The C-terminal extended proteins of mouse cFLIP-L (cellular FLICE-like apoptosisinhibitory protein) and human PNPO (pyridoxamine 5-phosphate oxidase) and HSD3B2 (3-hydroxysteroid dehydrogenase type II) are ubiquitylated and degraded, involving an E3 ligase, TRIM21, for cFLIP-L and PNPO degradation.</p>
<p><bold>Conclusion:</bold>
 Read-through mutant cFLIP-L, PNPO, and HSD3B2 are degraded by the ubiquitin-proteasome system.</p>
<p><bold>Significance:</bold>
 Degradation of read-through mutant proteins may cause hereditary disorders.</p>
</abstract>
<abstract><p>During translation, stop codon read-through occasionally happens when the stop codon is misread, skipped, or mutated, resulting in the production of aberrant proteins with C-terminal extension. These extended proteins are potentially deleterious, but their regulation is poorly understood. Here we show <italic>in vitro</italic>
 and <italic>in vivo</italic>
 evidence that mouse cFLIP-L with a 46-amino acid extension encoded by a read-through mutant gene is rapidly degraded by the ubiquitin-proteasome system, causing hepatocyte apoptosis during embryogenesis. The extended peptide interacts with an E3 ubiquitin ligase, TRIM21, to induce ubiquitylation of the mutant protein. In humans, 20 read-through mutations are related to hereditary disorders, and extended peptides found in human PNPO and HSD3B2 similarly destabilize these proteins, involving TRIM21 for PNPO degradation. Our findings indicate that degradation of aberrant proteins with C-terminal extension encoded by read-through mutant genes is a mechanism for loss of function resulting in hereditary disorders.</p>
</abstract>
<kwd-group><kwd>apoptosis</kwd>
<kwd>mutagenesis</kwd>
<kwd>proteasome</kwd>
<kwd>ubiquitin</kwd>
<kwd>ubiquitylation (ubiquitination)</kwd>
<kwd>HSD3B2</kwd>
<kwd>PNPO</kwd>
<kwd>TRIM21</kwd>
<kwd>cFLIP-L</kwd>
<kwd>read-through mutation</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/LymphedemaV1/Data/Pmc/Corpus

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000282 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000282 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Sante
   |area=    LymphedemaV1
   |flux=    Pmc
   |étape=   Corpus
   |type=    RBID
   |clé=     PMC:4653699
   |texte=   Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders*
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/RBID.i   -Sk "pubmed:26442586" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd   \
       | NlmPubMed2Wicri -a LymphedemaV1

This area was generated with Dilib version V0.6.31.
Data generation: Sat Nov 4 17:40:35 2017. Site generation: Tue Feb 13 16:42:16 2024

	Serveur d'exploration sur le lymphœdème
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur le lymphœdème

Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders*

Degradation of Stop Codon Read-through Mutant Proteins via the Ubiquitin-Proteasome System Causes Hereditary Disorders*

Source :

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki