The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins
Calnexin and calreticulin are homologous lectin chaperones that assist maturation of cellular and viral glycoproteins in the mammalian endoplasmic reticulum. Calnexin and calreticulin share the same specificity for monoglucosylated protein-bound N -glycans but associate with a distinct set of newly...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-08, Vol.280 (31), p.28265-28271 |
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| container_end_page | 28271 |
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| container_issue | 31 |
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| container_title | The Journal of biological chemistry |
| container_volume | 280 |
| creator | Pieren, Michel Galli, Carmela Denzel, Angela Molinari, Maurizio |
| description | Calnexin and calreticulin are homologous lectin chaperones that assist maturation of cellular and viral glycoproteins in the
mammalian endoplasmic reticulum. Calnexin and calreticulin share the same specificity for monoglucosylated protein-bound N -glycans but associate with a distinct set of newly synthesized polypeptides. We report here that most calnexin substrates
do not associate with calreticulin even upon selective calnexin inactivation, while BiP associates more abundantly with nascent
polypeptides under these conditions. Calreticulin associated more abundantly with orphan calnexin substrates only in infected
cells and preferentially with polypeptides of viral origin, showing stronger dependence of model viral glycoproteins on endoplasmic
reticulum lectins. This may explain why inactivation of the calnexin cycle affects viral replication and infectivity but not
viability of mammalian cells. |
| doi_str_mv | 10.1074/jbc.M501020200 |
| format | Article |
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mammalian endoplasmic reticulum. Calnexin and calreticulin share the same specificity for monoglucosylated protein-bound N -glycans but associate with a distinct set of newly synthesized polypeptides. We report here that most calnexin substrates
do not associate with calreticulin even upon selective calnexin inactivation, while BiP associates more abundantly with nascent
polypeptides under these conditions. Calreticulin associated more abundantly with orphan calnexin substrates only in infected
cells and preferentially with polypeptides of viral origin, showing stronger dependence of model viral glycoproteins on endoplasmic
reticulum lectins. This may explain why inactivation of the calnexin cycle affects viral replication and infectivity but not
viability of mammalian cells.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M501020200</identifier><identifier>PMID: 15951445</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amyloid Precursor Protein Secretases ; Animals ; Aspartic Acid Endopeptidases - metabolism ; Calnexin - genetics ; Calnexin - metabolism ; Calreticulin - metabolism ; Cell Line ; Cell Survival ; Endopeptidases ; Endoplasmic Reticulum - metabolism ; Fibroblasts - metabolism ; Fluorescent Antibody Technique, Indirect ; Glycoproteins - metabolism ; Mice ; Polysaccharides - metabolism ; Semliki forest virus - metabolism ; Semliki forest virus - physiology ; Substrate Specificity ; Vesicular stomatitis Indiana virus - metabolism ; Vesicular stomatitis Indiana virus - physiology ; Viral Plaque Assay ; Viral Proteins - metabolism ; Virus Replication</subject><ispartof>The Journal of biological chemistry, 2005-08, Vol.280 (31), p.28265-28271</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-612c4d0e2b569faabc9b8aaf98d3114df63caef3f20a2b0c57b076c719b66a693</citedby><cites>FETCH-LOGICAL-c393t-612c4d0e2b569faabc9b8aaf98d3114df63caef3f20a2b0c57b076c719b66a693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15951445$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pieren, Michel</creatorcontrib><creatorcontrib>Galli, Carmela</creatorcontrib><creatorcontrib>Denzel, Angela</creatorcontrib><creatorcontrib>Molinari, Maurizio</creatorcontrib><title>The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Calnexin and calreticulin are homologous lectin chaperones that assist maturation of cellular and viral glycoproteins in the
mammalian endoplasmic reticulum. Calnexin and calreticulin share the same specificity for monoglucosylated protein-bound N -glycans but associate with a distinct set of newly synthesized polypeptides. We report here that most calnexin substrates
do not associate with calreticulin even upon selective calnexin inactivation, while BiP associates more abundantly with nascent
polypeptides under these conditions. Calreticulin associated more abundantly with orphan calnexin substrates only in infected
cells and preferentially with polypeptides of viral origin, showing stronger dependence of model viral glycoproteins on endoplasmic
reticulum lectins. This may explain why inactivation of the calnexin cycle affects viral replication and infectivity but not
viability of mammalian cells.</description><subject>Amyloid Precursor Protein Secretases</subject><subject>Animals</subject><subject>Aspartic Acid Endopeptidases - metabolism</subject><subject>Calnexin - genetics</subject><subject>Calnexin - metabolism</subject><subject>Calreticulin - metabolism</subject><subject>Cell Line</subject><subject>Cell Survival</subject><subject>Endopeptidases</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fibroblasts - metabolism</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>Glycoproteins - metabolism</subject><subject>Mice</subject><subject>Polysaccharides - metabolism</subject><subject>Semliki forest virus - metabolism</subject><subject>Semliki forest virus - physiology</subject><subject>Substrate Specificity</subject><subject>Vesicular stomatitis Indiana virus - metabolism</subject><subject>Vesicular stomatitis Indiana virus - physiology</subject><subject>Viral Plaque Assay</subject><subject>Viral Proteins - metabolism</subject><subject>Virus Replication</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EoqWwMqIMiC3FZ8dOPKIKWqQilhaxWbbjUFdpAnYi6L_HpZU6cjec7u65D70IXQMeA86z-7U24xeGAZPo-AQNARc0pQzeT9EQYwKpIKwYoIsQ1jhaJuAcDYAJBlnGhmi2WNlkGWzSVslE1Y39cU2imnKXeNs509exoLfJxNZ1Xyv_13xzXtXJtN6a9tO3nXVNuERnlaqDvTrEEVo-PS4ms3T-On2ePMxTQwXtUg7EZCW2RDMuKqW0EbpQqhJFSQGysuLUKFvRimBFNDYs1zjnJgehOVdc0BG62--Nh796Gzq5ccHE51Rj2z5IXmREsDz_F4ScMSAMR3C8B41vQ_C2kp_ebZTfSsByJ7KMIsujyHHg5rC51xtbHvGDqhG43QMr97H6dt5K7VqzshtJCiwpxEA4o78_KoMj</recordid><startdate>20050805</startdate><enddate>20050805</enddate><creator>Pieren, Michel</creator><creator>Galli, Carmela</creator><creator>Denzel, Angela</creator><creator>Molinari, Maurizio</creator><general>American Society for Biochemistry and Molecular Biology</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20050805</creationdate><title>The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins</title><author>Pieren, Michel ; Galli, Carmela ; Denzel, Angela ; Molinari, Maurizio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-612c4d0e2b569faabc9b8aaf98d3114df63caef3f20a2b0c57b076c719b66a693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amyloid Precursor Protein Secretases</topic><topic>Animals</topic><topic>Aspartic Acid Endopeptidases - metabolism</topic><topic>Calnexin - genetics</topic><topic>Calnexin - metabolism</topic><topic>Calreticulin - metabolism</topic><topic>Cell Line</topic><topic>Cell Survival</topic><topic>Endopeptidases</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fibroblasts - metabolism</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>Glycoproteins - metabolism</topic><topic>Mice</topic><topic>Polysaccharides - metabolism</topic><topic>Semliki forest virus - metabolism</topic><topic>Semliki forest virus - physiology</topic><topic>Substrate Specificity</topic><topic>Vesicular stomatitis Indiana virus - metabolism</topic><topic>Vesicular stomatitis Indiana virus - physiology</topic><topic>Viral Plaque Assay</topic><topic>Viral Proteins - metabolism</topic><topic>Virus Replication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pieren, Michel</creatorcontrib><creatorcontrib>Galli, Carmela</creatorcontrib><creatorcontrib>Denzel, Angela</creatorcontrib><creatorcontrib>Molinari, Maurizio</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pieren, Michel</au><au>Galli, Carmela</au><au>Denzel, Angela</au><au>Molinari, Maurizio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-08-05</date><risdate>2005</risdate><volume>280</volume><issue>31</issue><spage>28265</spage><epage>28271</epage><pages>28265-28271</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Calnexin and calreticulin are homologous lectin chaperones that assist maturation of cellular and viral glycoproteins in the
mammalian endoplasmic reticulum. Calnexin and calreticulin share the same specificity for monoglucosylated protein-bound N -glycans but associate with a distinct set of newly synthesized polypeptides. We report here that most calnexin substrates
do not associate with calreticulin even upon selective calnexin inactivation, while BiP associates more abundantly with nascent
polypeptides under these conditions. Calreticulin associated more abundantly with orphan calnexin substrates only in infected
cells and preferentially with polypeptides of viral origin, showing stronger dependence of model viral glycoproteins on endoplasmic
reticulum lectins. This may explain why inactivation of the calnexin cycle affects viral replication and infectivity but not
viability of mammalian cells.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15951445</pmid><doi>10.1074/jbc.M501020200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 2005-08, Vol.280 (31), p.28265-28271 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amyloid Precursor Protein Secretases Animals Aspartic Acid Endopeptidases - metabolism Calnexin - genetics Calnexin - metabolism Calreticulin - metabolism Cell Line Cell Survival Endopeptidases Endoplasmic Reticulum - metabolism Fibroblasts - metabolism Fluorescent Antibody Technique, Indirect Glycoproteins - metabolism Mice Polysaccharides - metabolism Semliki forest virus - metabolism Semliki forest virus - physiology Substrate Specificity Vesicular stomatitis Indiana virus - metabolism Vesicular stomatitis Indiana virus - physiology Viral Plaque Assay Viral Proteins - metabolism Virus Replication |
| title | The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins |
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