Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System
Identifieur interne : 002D76 ( Istex/Corpus ); précédent : 002D75; suivant : 002D77Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System
Auteurs : Sarah H. D Wilson ; Angela M. Bailey ; Craig R. Nourse ; Marie-Geneviève Mattei ; Jennifer A. ByrneSource :
- Genomics [ 0888-7543 ] ; 2001.
English descriptors
- KwdEn :
- Academic press, Alonso, Apical, Bait, Bene, Biol, Breast cancer, Breast carcinoma, Breast carcinoma cells, CRHSP28, CSPP28, Carcinoma, Cdna, Cell lines, Chem, Chromosome, Copy number, Copyright, Exocrine secretory granules, Exon, Genbank, Gene family, Genes chromosomes cancer, Genomics, Heterologous, Heterologous binding partners, Heterologous partners, Hf7c, Hf7c cells, Human breast carcinoma, Human chromosome, Hybridization, MAL, Mal2, Mal2 protein, Mal2 transcript, Mal2 transcript levels, Mal2 transcripts, Membrane microdomains, N8, Novel member, Other sequences, Pancreatic acinar cells, Plasmid, Protein, Proteolipid, Proteolipid family, Puertollano, R10, Skeletal muscle, Solid media, TPD52, Transcript, Transcript levels, breast carcinoma.
- Teeft :
- Academic press, Alonso, Apical, Bait, Bene, Biol, Breast cancer, Breast carcinoma, Breast carcinoma cells, Carcinoma, Cdna, Cell lines, Chem, Chromosome, Copy number, Copyright, Exocrine secretory granules, Exon, Genbank, Gene family, Genes chromosomes cancer, Genomics, Heterologous, Heterologous binding partners, Heterologous partners, Hf7c, Hf7c cells, Human breast carcinoma, Human chromosome, Hybridization, Mal2, Mal2 protein, Mal2 transcript, Mal2 transcript levels, Mal2 transcripts, Membrane microdomains, Novel member, Other sequences, Pancreatic acinar cells, Plasmid, Protein, Proteolipid, Proteolipid family, Puertollano, Skeletal muscle, Solid media, Transcript, Transcript levels.
Abstract
Abstract: The TPD52 (tumor protein D52)-like proteins are small coiled-coil motif-bearing proteins which were first identified though their expression in human breast carcinoma. TPD52-like proteins are known to interact in hetero-and homomeric fashions, but there are no known heterologous binding partners for these proteins. We now report the cloning of a novel member of the MAL proteolipid family, named MAL2, though its interaction with a TPD52L2 bait in a yeast two-hybrid screen. MAL2 is predicted to be 176 residues (19 kDa) with four transmembrane domains and is 35.8% identical to MAL, a proteolipid required in apical vesicle transport. The MAL2 prey bound all TPD52-like baits tested in the yeast two-hybrid system and in vitro translation of MAL2 produced a single 19-kDa 35S-labeled protein which specifically bound full-length GST–Tpd52 in GST pull-down assays. The gene MAL2, which was localized to human chromosomal band 8q23 and shown to consist of four exons, is predominantly expressed in human kidney, lung, and liver. Our study has therefore identified a novel member of the MAL proteolipid family and potentially implicates TPD52-like proteins in vesicle transport.
Url:
DOI: 10.1006/geno.2001.6610
Links to Exploration step
ISTEX:F2F23650EF49362A620CBD2E095599F9BBB8CD32Le document en format XML
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Nourse</name><affiliation><mods:affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</mods:affiliation></affiliation></author><author><name sortKey="Mattei, Marie Genevieve" sort="Mattei, Marie Genevieve" uniqKey="Mattei M" first="Marie-Geneviève" last="Mattei">Marie-Geneviève Mattei</name><affiliation><mods:affiliation>Unité 491 de Génétique Médicale et Développement de l'INSERM, Faculté de la Médecine de la Timone, 27 Boulevard Jean Moulin, Marseille Cedex, 13385, France</mods:affiliation></affiliation></author><author><name sortKey="Byrne, Jennifer A" sort="Byrne, Jennifer A" uniqKey="Byrne J" first="Jennifer A" last="Byrne">Jennifer A. Byrne</name><affiliation><mods:affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Genomics</title><title level="j" type="abbrev">YGENO</title><idno type="ISSN">0888-7543</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2001">2001</date><biblScope unit="volume">76</biblScope><biblScope unit="issue">1–3</biblScope><biblScope unit="page" from="81">81</biblScope><biblScope unit="page" to="88">88</biblScope></imprint><idno type="ISSN">0888-7543</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0888-7543</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Academic press</term><term>Alonso</term><term>Apical</term><term>Bait</term><term>Bene</term><term>Biol</term><term>Breast cancer</term><term>Breast carcinoma</term><term>Breast carcinoma cells</term><term>CRHSP28</term><term>CSPP28</term><term>Carcinoma</term><term>Cdna</term><term>Cell lines</term><term>Chem</term><term>Chromosome</term><term>Copy number</term><term>Copyright</term><term>Exocrine secretory granules</term><term>Exon</term><term>Genbank</term><term>Gene family</term><term>Genes chromosomes cancer</term><term>Genomics</term><term>Heterologous</term><term>Heterologous binding partners</term><term>Heterologous partners</term><term>Hf7c</term><term>Hf7c cells</term><term>Human breast carcinoma</term><term>Human chromosome</term><term>Hybridization</term><term>MAL</term><term>Mal2</term><term>Mal2 protein</term><term>Mal2 transcript</term><term>Mal2 transcript levels</term><term>Mal2 transcripts</term><term>Membrane microdomains</term><term>N8</term><term>Novel member</term><term>Other sequences</term><term>Pancreatic acinar cells</term><term>Plasmid</term><term>Protein</term><term>Proteolipid</term><term>Proteolipid family</term><term>Puertollano</term><term>R10</term><term>Skeletal muscle</term><term>Solid media</term><term>TPD52</term><term>Transcript</term><term>Transcript levels</term><term>breast carcinoma</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Alonso</term><term>Apical</term><term>Bait</term><term>Bene</term><term>Biol</term><term>Breast cancer</term><term>Breast carcinoma</term><term>Breast carcinoma cells</term><term>Carcinoma</term><term>Cdna</term><term>Cell lines</term><term>Chem</term><term>Chromosome</term><term>Copy number</term><term>Copyright</term><term>Exocrine secretory granules</term><term>Exon</term><term>Genbank</term><term>Gene family</term><term>Genes chromosomes cancer</term><term>Genomics</term><term>Heterologous</term><term>Heterologous binding partners</term><term>Heterologous partners</term><term>Hf7c</term><term>Hf7c cells</term><term>Human breast carcinoma</term><term>Human chromosome</term><term>Hybridization</term><term>Mal2</term><term>Mal2 protein</term><term>Mal2 transcript</term><term>Mal2 transcript levels</term><term>Mal2 transcripts</term><term>Membrane microdomains</term><term>Novel member</term><term>Other sequences</term><term>Pancreatic acinar cells</term><term>Plasmid</term><term>Protein</term><term>Proteolipid</term><term>Proteolipid family</term><term>Puertollano</term><term>Skeletal muscle</term><term>Solid media</term><term>Transcript</term><term>Transcript levels</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The TPD52 (tumor protein D52)-like proteins are small coiled-coil motif-bearing proteins which were first identified though their expression in human breast carcinoma. TPD52-like proteins are known to interact in hetero-and homomeric fashions, but there are no known heterologous binding partners for these proteins. We now report the cloning of a novel member of the MAL proteolipid family, named MAL2, though its interaction with a TPD52L2 bait in a yeast two-hybrid screen. MAL2 is predicted to be 176 residues (19 kDa) with four transmembrane domains and is 35.8% identical to MAL, a proteolipid required in apical vesicle transport. The MAL2 prey bound all TPD52-like baits tested in the yeast two-hybrid system and in vitro translation of MAL2 produced a single 19-kDa 35S-labeled protein which specifically bound full-length GST–Tpd52 in GST pull-down assays. The gene MAL2, which was localized to human chromosomal band 8q23 and shown to consist of four exons, is predominantly expressed in human kidney, lung, and liver. Our study has therefore identified a novel member of the MAL proteolipid family and potentially implicates TPD52-like proteins in vesicle transport.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>mal2</json:string><json:string>cdna</json:string><json:string>proteolipid</json:string><json:string>chromosome</json:string><json:string>alonso</json:string><json:string>carcinoma</json:string><json:string>apical</json:string><json:string>exon</json:string><json:string>bene</json:string><json:string>plasmid</json:string><json:string>biol</json:string><json:string>heterologous</json:string><json:string>hf7c</json:string><json:string>genomics</json:string><json:string>proteolipid family</json:string><json:string>academic press</json:string><json:string>copyright</json:string><json:string>chem</json:string><json:string>puertollano</json:string><json:string>genbank</json:string><json:string>human breast carcinoma</json:string><json:string>novel 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procedures</json:string><json:string>protein product sizes</json:string><json:string>autoradiographic film</json:string><json:string>bait plasmid</json:string><json:string>novel gene</json:string><json:string>comparative genomic hybridization</json:string><json:string>prey plasmid</json:string><json:string>days incubation</json:string><json:string>membrane</json:string><json:string>yeast</json:string></teeft></keywords><author><json:item><name>Sarah H.D Wilson</name><affiliations><json:string>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</json:string></affiliations></json:item><json:item><name>Angela M Bailey</name><affiliations><json:string>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</json:string></affiliations></json:item><json:item><name>Craig R Nourse</name><affiliations><json:string>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</json:string></affiliations></json:item><json:item><name>Marie-Geneviève Mattei</name><affiliations><json:string>Unité 491 de Génétique Médicale et Développement de l'INSERM, Faculté de la Médecine de la Timone, 27 Boulevard Jean Moulin, Marseille Cedex, 13385, France</json:string></affiliations></json:item><json:item><name>Jennifer A Byrne</name><affiliations><json:string>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>breast carcinoma</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>TPD52</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>N8</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>R10</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CSPP28</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CRHSP28</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>MAL</value></json:item></subject><arkIstex>ark:/67375/6H6-S86SZWPK-F</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The TPD52 (tumor protein D52)-like proteins are small coiled-coil motif-bearing proteins which were first identified though their expression in human breast carcinoma. TPD52-like proteins are known to interact in hetero-and homomeric fashions, but there are no known heterologous binding partners for these proteins. We now report the cloning of a novel member of the MAL proteolipid family, named MAL2, though its interaction with a TPD52L2 bait in a yeast two-hybrid screen. MAL2 is predicted to be 176 residues (19 kDa) with four transmembrane domains and is 35.8% identical to MAL, a proteolipid required in apical vesicle transport. The MAL2 prey bound all TPD52-like baits tested in the yeast two-hybrid system and in vitro translation of MAL2 produced a single 19-kDa 35S-labeled protein which specifically bound full-length GST–Tpd52 in GST pull-down assays. The gene MAL2, which was localized to human chromosomal band 8q23 and shown to consist of four exons, is predominantly expressed in human kidney, lung, and liver. Our study has therefore identified a novel member of the MAL proteolipid family and potentially implicates TPD52-like proteins in vesicle transport.</abstract><qualityIndicators><score>9.16</score><pdfWordCount>6905</pdfWordCount><pdfCharCount>44070</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>519.307 x 731.976 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>180</abstractWordCount><abstractCharCount>1188</abstractCharCount><keywordCount>7</keywordCount></qualityIndicators><title>Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System</title><pmid><json:string>11549320</json:string></pmid><pii><json:string>S0888-7543(01)96610-8</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Genomics</title><language><json:string>unknown</json:string></language><publicationDate>2001</publicationDate><issn><json:string>0888-7543</json:string></issn><pii><json:string>S0888-7543(00)X0207-8</json:string></pii><volume>76</volume><issue>1–3</issue><pages><first>81</first><last>88</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>2001</json:string><json:string>35S</json:string><json:string>2751</json:string></date><geogName></geogName><orgName><json:string>Oncology Department of the Children</json:string><json:string>University of Sydney, Australia</json:string><json:string>Australia Unité</json:string><json:string>University of Sydney Department of Paediatrics and Child</json:string><json:string>Biotech</json:string><json:string>Vector Laboratories</json:string><json:string>Clontech</json:string><json:string>Oncology Children’s Foundation</json:string><json:string>National Health and Medical Research</json:string><json:string>Promega Corp.</json:string><json:string>American Type Culture Collection Catalogue</json:string><json:string>Kathleen Cuningham Foundation for Breast Cancer Research</json:string><json:string>Children</json:string></orgName><orgName_funder><json:string>Kathleen Cuningham Foundation for Breast Cancer Research</json:string><json:string>Children</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Merlin Crossley</json:string><json:string>Rancaño</json:string><json:string>Jennifer A. Byrne</json:string><json:string>Angela M. Bailey</json:string><json:string>Jean Moulin</json:string><json:string>Miguel Alonso</json:string><json:string>Danielle Depetris</json:string><json:string>Marie-Geneviève Mattei</json:string><json:string>C. Matrixes</json:string><json:string>C. Proteins</json:string><json:string>Craig R. 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science</json:string><json:string>2 - genetics & heredity</json:string><json:string>2 - biotechnology & applied microbiology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - genetics & heredity</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Genetics</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - industries agroalimentaires</json:string></inist></categories><publicationDate>2001</publicationDate><copyrightDate>2001</copyrightDate><doi><json:string>10.1006/geno.2001.6610</json:string></doi><id>F2F23650EF49362A620CBD2E095599F9BBB8CD32</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/F2F23650EF49362A620CBD2E095599F9BBB8CD32/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/F2F23650EF49362A620CBD2E095599F9BBB8CD32/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/F2F23650EF49362A620CBD2E095599F9BBB8CD32/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>©2001 Elsevier Science (USA)</p></availability><date>2001</date></publicationStmt><notesStmt><note type="content">Section title: Regular Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System</title><author xml:id="author-0000"><persName><forename type="first">Sarah H.D</forename><surname>Wilson</surname></persName><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Angela M</forename><surname>Bailey</surname></persName><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Craig R</forename><surname>Nourse</surname></persName><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Marie-Geneviève</forename><surname>Mattei</surname></persName><affiliation>Unité 491 de Génétique Médicale et Développement de l'INSERM, Faculté de la Médecine de la Timone, 27 Boulevard Jean Moulin, Marseille Cedex, 13385, France</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Jennifer A</forename><surname>Byrne</surname></persName><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation></author><idno type="istex">F2F23650EF49362A620CBD2E095599F9BBB8CD32</idno><idno type="DOI">10.1006/geno.2001.6610</idno><idno type="PII">S0888-7543(01)96610-8</idno></analytic><monogr><title level="j">Genomics</title><title level="j" type="abbrev">YGENO</title><idno type="pISSN">0888-7543</idno><idno type="PII">S0888-7543(00)X0207-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2001"></date><biblScope unit="volume">76</biblScope><biblScope unit="issue">1–3</biblScope><biblScope unit="page" from="81">81</biblScope><biblScope unit="page" to="88">88</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2001</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The TPD52 (tumor protein D52)-like proteins are small coiled-coil motif-bearing proteins which were first identified though their expression in human breast carcinoma. TPD52-like proteins are known to interact in hetero-and homomeric fashions, but there are no known heterologous binding partners for these proteins. We now report the cloning of a novel member of the MAL proteolipid family, named MAL2, though its interaction with a TPD52L2 bait in a yeast two-hybrid screen. MAL2 is predicted to be 176 residues (19 kDa) with four transmembrane domains and is 35.8% identical to MAL, a proteolipid required in apical vesicle transport. The MAL2 prey bound all TPD52-like baits tested in the yeast two-hybrid system and in vitro translation of MAL2 produced a single 19-kDa 35S-labeled protein which specifically bound full-length GST–Tpd52 in GST pull-down assays. The gene MAL2, which was localized to human chromosomal band 8q23 and shown to consist of four exons, is predominantly expressed in human kidney, lung, and liver. Our study has therefore identified a novel member of the MAL proteolipid family and potentially implicates TPD52-like proteins in vesicle transport.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>breast carcinoma</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>TPD52</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>N8</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>R10</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>CSPP28</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>CRHSP28</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>MAL</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2001">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/F2F23650EF49362A620CBD2E095599F9BBB8CD32/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YGENO</jid><aid>96610</aid><ce:pii>S0888-7543(01)96610-8</ce:pii><ce:doi>10.1006/geno.2001.6610</ce:doi><ce:copyright type="full-transfer" year="2001">Elsevier Science (USA)</ce:copyright></item-info><head><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System</ce:title><ce:author-group><ce:author><ce:given-name>Sarah H.D</ce:given-name><ce:surname>Wilson</ce:surname><ce:cross-ref refid="A0"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Angela M</ce:given-name><ce:surname>Bailey</ce:surname><ce:cross-ref refid="A0"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Craig R</ce:given-name><ce:surname>Nourse</ce:surname><ce:cross-ref refid="A0"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Marie-Geneviève</ce:given-name><ce:surname>Mattei</ce:surname><ce:cross-ref refid="A1"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jennifer A</ce:given-name><ce:surname>Byrne</ce:surname><ce:cross-ref refid="A0"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="A2"><ce:sup>c</ce:sup></ce:cross-ref><ce:cross-ref refid="FNAST">*<ce:footnote id="FNAST"><ce:label>*</ce:label><ce:note-para>To whom correspondence and reprint requests should be addressed. Fax: +61 2 9845 3078. E-mail: JennifeB@chw.edu.au.</ce:note-para></ce:footnote></ce:cross-ref></ce:author><ce:affiliation id="A0"><ce:label>a</ce:label><ce:textfn>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</ce:textfn></ce:affiliation><ce:affiliation id="A1"><ce:label>b</ce:label><ce:textfn>Unité 491 de Génétique Médicale et Développement de l'INSERM, Faculté de la Médecine de la Timone, 27 Boulevard Jean Moulin, Marseille Cedex, 13385, France</ce:textfn></ce:affiliation><ce:affiliation id="A2"><ce:label>c</ce:label><ce:textfn>The University of Sydney Department of Paediatrics and Child Health, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="6" month="3" year="2001"></ce:date-received><ce:date-accepted day="26" month="6" year="2001"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The TPD52 (tumor protein D52)-like proteins are small coiled-coil motif-bearing proteins which were first identified though their expression in human breast carcinoma. TPD52-like proteins are known to interact in hetero-and homomeric fashions, but there are no known heterologous binding partners for these proteins. We now report the cloning of a novel member of the MAL proteolipid family, named MAL2, though its interaction with a TPD52L2 bait in a yeast two-hybrid screen. MAL2 is predicted to be 176 residues (19 kDa) with four transmembrane domains and is 35.8% identical to MAL, a proteolipid required in apical vesicle transport. The MAL2 prey bound all TPD52-like baits tested in the yeast two-hybrid system and <ce:italic>in vitro</ce:italic> translation of <ce:italic>MAL2</ce:italic> produced a single 19-kDa <ce:sup>35</ce:sup>S-labeled protein which specifically bound full-length GST–Tpd52 in GST pull-down assays. The gene <ce:italic>MAL2</ce:italic>, which was localized to human chromosomal band 8q23 and shown to consist of four exons, is predominantly expressed in human kidney, lung, and liver. Our study has therefore identified a novel member of the MAL proteolipid family and potentially implicates TPD52-like proteins in vesicle transport.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>breast carcinoma</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>TPD52</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>N8</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>R10</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>CSPP28</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>CRHSP28</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>MAL</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Identification of MAL2, a Novel Member of the MAL Proteolipid Family, Though Interactions with TPD52-like Proteins in the Yeast Two-Hybrid System</title></titleInfo><name type="personal"><namePart type="given">Sarah H.D</namePart><namePart type="family">Wilson</namePart><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Angela M</namePart><namePart type="family">Bailey</namePart><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Craig R</namePart><namePart type="family">Nourse</namePart><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Marie-Geneviève</namePart><namePart type="family">Mattei</namePart><affiliation>Unité 491 de Génétique Médicale et Développement de l'INSERM, Faculté de la Médecine de la Timone, 27 Boulevard Jean Moulin, Marseille Cedex, 13385, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jennifer A</namePart><namePart type="family">Byrne</namePart><affiliation>Molecular Oncology Laboratory, Oncology Research Unit, The Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW, 2145, Australia</affiliation><description>To whom correspondence and reprint requests should be addressed. Fax: +61 2 9845 3078. E-mail: JennifeB@chw.edu.au.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">2001</dateIssued><copyrightDate encoding="w3cdtf">2001</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The TPD52 (tumor protein D52)-like proteins are small coiled-coil motif-bearing proteins which were first identified though their expression in human breast carcinoma. TPD52-like proteins are known to interact in hetero-and homomeric fashions, but there are no known heterologous binding partners for these proteins. We now report the cloning of a novel member of the MAL proteolipid family, named MAL2, though its interaction with a TPD52L2 bait in a yeast two-hybrid screen. MAL2 is predicted to be 176 residues (19 kDa) with four transmembrane domains and is 35.8% identical to MAL, a proteolipid required in apical vesicle transport. The MAL2 prey bound all TPD52-like baits tested in the yeast two-hybrid system and in vitro translation of MAL2 produced a single 19-kDa 35S-labeled protein which specifically bound full-length GST–Tpd52 in GST pull-down assays. The gene MAL2, which was localized to human chromosomal band 8q23 and shown to consist of four exons, is predominantly expressed in human kidney, lung, and liver. Our study has therefore identified a novel member of the MAL proteolipid family and potentially implicates TPD52-like proteins in vesicle transport.</abstract><note type="content">Section title: Regular Article</note><subject lang="en"><genre>Abbreviations</genre><topic>breast carcinoma</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>TPD52</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>N8</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>R10</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>CSPP28</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>CRHSP28</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>MAL</topic></subject><relatedItem type="host"><titleInfo><title>Genomics</title></titleInfo><titleInfo type="abbreviated"><title>YGENO</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">200108</dateIssued></originInfo><identifier type="ISSN">0888-7543</identifier><identifier type="PII">S0888-7543(00)X0207-8</identifier><part><date>200108</date><detail type="volume"><number>76</number><caption>vol.</caption></detail><detail type="issue"><number>1–3</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>125</end></extent><extent unit="pages"><start>81</start><end>88</end></extent></part></relatedItem><identifier type="istex">F2F23650EF49362A620CBD2E095599F9BBB8CD32</identifier><identifier type="ark">ark:/67375/6H6-S86SZWPK-F</identifier><identifier type="DOI">10.1006/geno.2001.6610</identifier><identifier type="PII">S0888-7543(01)96610-8</identifier><accessCondition type="use and reproduction" contentType="copyright">©2001 Elsevier Science (USA)</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Elsevier Science (USA), ©2001</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/F2F23650EF49362A620CBD2E095599F9BBB8CD32/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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