Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs
Identifieur interne : 002697 ( Istex/Corpus ); précédent : 002696; suivant : 002698Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs
Auteurs : Shu-Hui Liu ; Mei Lie Wong ; Charles S. Craik ; Frances M. BrodskySource :
- Cell [ 0092-8674 ] ; 1995.
English descriptors
- Teeft :
- Adaptor, Adaptor molecules, Affinity resin, Antibody binding, Bacterial lysate, Binding buffer, Binding sites, Biol, Bovine, Bovine brain clathrin, Bovine clathrin, Brodsky, Cdna, Cell biol, Chain sequence, Clathrin, Clathrin assembly, Clathrin lattice, Clathrin light chains, Clathrin triskelion, Clathrin triskelions, Coexpressed, Deletion, Deletion mutagenesis, Electron microscopy, Fragment, Fragments coexpressed, Fusion proteins, Heavy chain, Heavy chain fragment, Kirchhausen, Lattice, Light chain, Light chain binding, Light chains, Light region, Light sites, Lysate, Marker proteins, Mutant, Nathke, Parham, Peak fraction, Previous studies, Recombinant, Recombinant proteins, Residue, Size exclusion chromatography, Trimer, Trimerization, Trimerization domain, Triskelion, Triskelion vertex, Ungewickell, Uranyl acetate, Vesicle, Whole triskelion.
Abstract
Abstract: Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.
Url:
DOI: 10.1016/0092-8674(95)90167-1
Links to Exploration step
ISTEX:88AF3341FD0CDD2F45F5B4B176A881DDE5271C3BLe document en format XML
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W. Hooper Foundation Department of Microbiology and Immunology School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</json:string></affiliations></json:item><json:item><name>Mei Lie Wong</name><affiliations><json:string>Department of Biochemistry and Biophysics Howard Hughes Medical Institute School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</json:string></affiliations></json:item><json:item><name>Charles S. Craik</name><affiliations><json:string>Department of Pharmaceutical Chemistry School of Pharmacy and Department of Biochemistry and Biophysics School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</json:string></affiliations></json:item><json:item><name>Frances M. Brodsky</name><affiliations><json:string>Departments of Pharmacy and Pharmaceutical Chemistry School of Pharmacy and G. W. Hooper Foundation Department of Microbiology and Immunology School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-3KJ6BST1-F</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.</abstract><qualityIndicators><score>8.38</score><pdfWordCount>6150</pdfWordCount><pdfCharCount>51095</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>115</abstractWordCount><abstractCharCount>875</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs</title><pmid><json:string>7585943</json:string></pmid><pii><json:string>0092-8674(95)90167-1</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. 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Brodsky</json:string><json:string>P. Parham</json:string><json:string>A. Wilde</json:string><json:string>Parham</json:string><json:string>H. Nelson</json:string><json:string>R. Cerpa</json:string><json:string>D. Riethof</json:string><json:string>L. Koren</json:string><json:string>Charles S. Craik</json:string><json:string>W. Mallet</json:string><json:string>Biophysics School</json:string><json:string>S. Morris</json:string></persName><placeName><json:string>Bradford</json:string><json:string>Mannheim</json:string><json:string>San Francisco</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Sanger et al., 1977</json:string><json:string>Kirchhausen and Harrison, 1984</json:string><json:string>Keen, 1990</json:string><json:string>Nathans and Hogness, 1983</json:string><json:string>Adams et al., 1993</json:string><json:string>Garnier et al., 1978</json:string><json:string>Manfredi and Bazari, 1987</json:string><json:string>Wilson et al., 1994 C</json:string><json:string>Nlthke et al., 1992</json:string><json:string>Kirchhausen et al., 1983</json:string><json:string>Keen et al., 1991</json:string><json:string>Blank and Brodsky, 1986</json:string><json:string>Bazinet et al., 1993</json:string><json:string>Nathke et al., 1992</json:string><json:string>Chou and Fasman, 1978</json:string><json:string>Ungewickell and Ungewickell, 1991</json:string><json:string>Brodsky et al., 1983</json:string><json:string>Ungewickell and Branton, 1981</json:string><json:string>Dodge et al., 1991</json:string><json:string>Kirchhausen et al. 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Hooper Foundation Department of Microbiology and Immunology School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Mei Lie</forename><surname>Wong</surname></persName><affiliation>Department of Biochemistry and Biophysics Howard Hughes Medical Institute School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Charles S.</forename><surname>Craik</surname></persName><affiliation>Department of Pharmaceutical Chemistry School of Pharmacy and Department of Biochemistry and Biophysics School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Frances M.</forename><surname>Brodsky</surname></persName><affiliation>Departments of Pharmacy and Pharmaceutical Chemistry School of Pharmacy and G. W. Hooper Foundation Department of Microbiology and Immunology School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation></author><idno type="istex">88AF3341FD0CDD2F45F5B4B176A881DDE5271C3B</idno><idno type="ark">ark:/67375/6H6-3KJ6BST1-F</idno><idno type="DOI">10.1016/0092-8674(95)90167-1</idno><idno type="PII">0092-8674(95)90167-1</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0436-9</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995"></date><biblScope unit="volume">83</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="257">257</biblScope><biblScope unit="page" to="267">267</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.</p></abstract></profileDesc><revisionDesc><change when="1995-08-22">Modified</change><change when="1995">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-3KJ6BST1-F/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"><item-info><jid>CELL</jid><aid>95901671</aid><ce:pii>0092-8674(95)90167-1</ce:pii><ce:doi>10.1016/0092-8674(95)90167-1</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs</ce:title><ce:author-group><ce:author><ce:given-name>Shu-Hui</ce:given-name><ce:surname>Liu</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Mei Lie</ce:given-name><ce:surname>Wong</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Charles S.</ce:given-name><ce:surname>Craik</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Frances M.</ce:given-name><ce:surname>Brodsky</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>∗</ce:label><ce:textfn>Departments of Pharmacy and Pharmaceutical Chemistry School of Pharmacy and G. W. Hooper Foundation Department of Microbiology and Immunology School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>†</ce:label><ce:textfn>Department of Biochemistry and Biophysics Howard Hughes Medical Institute School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>‡</ce:label><ce:textfn>Department of Pharmaceutical Chemistry School of Pharmacy and Department of Biochemistry and Biophysics School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="12" month="7" year="1995"></ce:date-received><ce:date-revised day="22" month="8" year="1995"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs</title></titleInfo><name type="personal"><namePart type="given">Shu-Hui</namePart><namePart type="family">Liu</namePart><affiliation>Departments of Pharmacy and Pharmaceutical Chemistry School of Pharmacy and G. W. Hooper Foundation Department of Microbiology and Immunology School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Mei Lie</namePart><namePart type="family">Wong</namePart><affiliation>Department of Biochemistry and Biophysics Howard Hughes Medical Institute School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Charles S.</namePart><namePart type="family">Craik</namePart><affiliation>Department of Pharmaceutical Chemistry School of Pharmacy and Department of Biochemistry and Biophysics School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Frances M.</namePart><namePart type="family">Brodsky</namePart><affiliation>Departments of Pharmacy and Pharmaceutical Chemistry School of Pharmacy and G. W. Hooper Foundation Department of Microbiology and Immunology School of Medicine University of California, San Francisco San Francisco, California 94143-0552, USA</affiliation><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">1995</dateIssued><dateModified encoding="w3cdtf">1995-08-22</dateModified><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</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">1995</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0436-9</identifier><part><date>1995</date><detail type="volume"><number>83</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>157</start><end>343</end></extent><extent unit="pages"><start>257</start><end>267</end></extent></part></relatedItem><identifier type="istex">88AF3341FD0CDD2F45F5B4B176A881DDE5271C3B</identifier><identifier type="ark">ark:/67375/6H6-3KJ6BST1-F</identifier><identifier type="DOI">10.1016/0092-8674(95)90167-1</identifier><identifier type="PII">0092-8674(95)90167-1</identifier><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></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-3KJ6BST1-F/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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