Coatomer Interaction with Di-Lysine Endoplasmic Reticulum Retention Motifs
Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1994-03, Vol.263 (5153), p.1629-1631 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Cosson, Pierre Letourneur, François |
| description | Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals. |
| doi_str_mv | 10.1126/science.8128252 |
| format | Article |
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Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. 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Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antiserum</subject><subject>Awards</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Transport</subject><subject>Cell Line</subject><subject>Chimeras</subject><subject>Coatomer Protein</subject><subject>COS cells</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - metabolism</subject><subject>Gels</subject><subject>Golgi Apparatus - metabolism</subject><subject>Goods and services tax</subject><subject>Hexosyltransferases</subject><subject>Life Sciences</subject><subject>Lysine - chemistry</subject><subject>Lysine - metabolism</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Physiological aspects</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Transferases - chemistry</subject><subject>Transferases - metabolism</subject><subject>Transmembrane proteins</subject><subject>Yeasts</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0kuP0zAQAOAIgZaycOYCUk8IpM2uH_Ejx1KWblGgEq-r5TqTrldJXGIH2H-PS6KiSpWofLA189mSZyZJnmN0iTHhV95YaA1cSkwkYeRBMsEoZ2lOEH2YTBCiPJVIsMfJE-_vEIq5nJ4lZyOfJB_mTgfXQDddtgE6bYJ17fSXDbfTdzYt7r1tYXrdlm5ba99YM_0MwZq-7pvdCdq__KMLtvJPk0eVrj08G_fz5Nv766_zm7RYLZbzWZEazmhIMUeizATjDDOmS8zWbM2RkaSktGRYi8qgkgjgFchS0hjWGZBcgAApUFbR8-TN8O6trtW2s43u7pXTVt3MCrWLxV_jDCH8E0f7arDbzv3owQfVWG-grnULrvdKcJpTKdF_IeYyoyyjEV4McKNrULatXIhV20Abi1e7FiobwzOc5ZmghESeHuFxlRCrecy_PvCRBPgdNrr3Xi2_fDqZrr6fTN8uTqVyURzQi2PUuLqGDajY9PnqgF8N3HTO-w6qffMwUrthVuMwq3E6442XY1P6dQPl3v_Lvxjydz64bp8mUlLOBf0DApPz7w</recordid><startdate>19940318</startdate><enddate>19940318</enddate><creator>Cosson, Pierre</creator><creator>Letourneur, François</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>American Association for the Advancement of Science (AAAS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>M7N</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>19940318</creationdate><title>Coatomer Interaction with Di-Lysine Endoplasmic Reticulum Retention Motifs</title><author>Cosson, Pierre ; Letourneur, François</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c653t-1607d47565155ad15b5b60c82d33d51a7fc0d27e6fe8d832d3a4e297e7e8704f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antiserum</topic><topic>Awards</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological Transport</topic><topic>Cell Line</topic><topic>Chimeras</topic><topic>Coatomer Protein</topic><topic>COS cells</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - metabolism</topic><topic>Gels</topic><topic>Golgi Apparatus - metabolism</topic><topic>Goods and services tax</topic><topic>Hexosyltransferases</topic><topic>Life Sciences</topic><topic>Lysine - chemistry</topic><topic>Lysine - metabolism</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Physiological aspects</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Transferases - chemistry</topic><topic>Transferases - metabolism</topic><topic>Transmembrane proteins</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cosson, Pierre</creatorcontrib><creatorcontrib>Letourneur, François</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: High School</collection><collection>Gale In Context: Biography</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Canada</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cosson, Pierre</au><au>Letourneur, François</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Coatomer Interaction with Di-Lysine Endoplasmic Reticulum Retention Motifs</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1994-03-18</date><risdate>1994</risdate><volume>263</volume><issue>5153</issue><spage>1629</spage><epage>1631</epage><pages>1629-1631</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>Although signals for retention in the endoplasmic reticulum (ER) have been identified in the cytoplasmic domain of various ER-resident type I transmembrane proteins, the mechanisms responsible for ER retention are still unknown. Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals.</abstract><cop>United States</cop><pub>American Society for the Advancement of Science</pub><pmid>8128252</pmid><doi>10.1126/science.8128252</doi><tpages>3</tpages></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 1994-03, Vol.263 (5153), p.1629-1631 |
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| language | eng |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Amino Acid Sequence Animals Antibodies Antiserum Awards Biochemistry, Molecular Biology Biological Transport Cell Line Chimeras Coatomer Protein COS cells Endoplasmic reticulum Endoplasmic Reticulum - metabolism Fungal Proteins - chemistry Fungal Proteins - metabolism Gels Golgi Apparatus - metabolism Goods and services tax Hexosyltransferases Life Sciences Lysine - chemistry Lysine - metabolism Membrane Proteins - metabolism Molecular Sequence Data Mutation Physiological aspects Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Transferases - chemistry Transferases - metabolism Transmembrane proteins Yeasts |
| title | Coatomer Interaction with Di-Lysine Endoplasmic Reticulum Retention Motifs |
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