The O-Glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells
Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of...
Gespeichert in:
| Veröffentlicht in: | The Journal of cell biology 1997-11, Vol.139 (4), p.929-940 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 940 |
|---|---|
| container_issue | 4 |
| container_start_page | 929 |
| container_title | The Journal of cell biology |
| container_volume | 139 |
| creator | Yeaman, Charles Le Gall, Annick H. Baldwin, Anne N. Monlauzeur, Laure Le Bivic, Andre Rodriguez-Boulan, Enrique |
| description | Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of transmembrane neurotrophin receptors (p75NTR) is localized to a juxtamembrane region of the extracellular domain that is rich in O-glycosylated serine/threonine residues. An internal deletion of 50 amino acids that removes this stalk domain from p75NTR causes the protein to be sorted exclusively of the basolateral plasma membrane. Basolateral sorting stalk-minus p75NTR does not occur by default, but requires sequences present in the cytoplasmic domain. The stalk domain is also required for apical secretion of a soluble form of p75NTR, providing the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well as secreted protein. However, the single N-glycan present on p75NTR is not required for apical sorting of either transmembrane or secreted forms. |
| doi_str_mv | 10.1083/jcb.139.4.929 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2139957</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1618284</jstor_id><sourcerecordid>1618284</sourcerecordid><originalsourceid>FETCH-LOGICAL-c496t-334a61c0181ecaa721320b05b99c74a78212bfb1f22cf640e27b87923f4b9b33</originalsourceid><addsrcrecordid>eNpdkUFvEzEQhS0EKmnhyA0kq4feNvXY3rV9QapSKBWFojZ3y3a9jcNmvbV3kcKvx1WiAj2NRu_5mxk_hN4BmQOR7HTt7ByYmvO5ouoFmkHNSSWBk5doRgiFStW0fo0Oc14TQrjg7AAdKNbQGmCGhuXK4-vqotu6mLedGf0dvh1N9xOfx40JPb7M-MY_TCEVoY0Jnw3BmQ7fxjSG_h7HFn_3U4pjisOq2G-888MYU8al-RE7k8Lv8vLb-eIrXviuy2_Qq9Z02b_d1yO0_PxpufhSXV1fXC7OrirHVTNWjHHTgCMgwTtjBAVGiSW1VcoJboSkQG1roaXUtQ0nngorhaKs5VZZxo7Qxx12mOzG3znfj8l0ekhhY9JWRxP0_0ofVvo-_tJlkFK1KICTPSDFh8nnUW9CduUC0_s4ZS0UB6glKcbjZ8Z1nFJfbissQaTk8EirdiaXYs7Jt0-bANGPMeoSoy6jNdclxuL_8O_6T-59bkV_v9PXuXz2X1gDkkrO_gCQx6JN</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217088417</pqid></control><display><type>article</type><title>The O-Glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Yeaman, Charles ; Le Gall, Annick H. ; Baldwin, Anne N. ; Monlauzeur, Laure ; Le Bivic, Andre ; Rodriguez-Boulan, Enrique</creator><creatorcontrib>Yeaman, Charles ; Le Gall, Annick H. ; Baldwin, Anne N. ; Monlauzeur, Laure ; Le Bivic, Andre ; Rodriguez-Boulan, Enrique</creatorcontrib><description>Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of transmembrane neurotrophin receptors (p75NTR) is localized to a juxtamembrane region of the extracellular domain that is rich in O-glycosylated serine/threonine residues. An internal deletion of 50 amino acids that removes this stalk domain from p75NTR causes the protein to be sorted exclusively of the basolateral plasma membrane. Basolateral sorting stalk-minus p75NTR does not occur by default, but requires sequences present in the cytoplasmic domain. The stalk domain is also required for apical secretion of a soluble form of p75NTR, providing the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well as secreted protein. However, the single N-glycan present on p75NTR is not required for apical sorting of either transmembrane or secreted forms.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.139.4.929</identifier><identifier>PMID: 9362511</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Amino acids ; Animals ; Asparagine - chemistry ; Cell Line ; Cell lines ; Cell membranes ; Cell Polarity ; Cells ; Cellular biology ; Cytoplasm - chemistry ; Cytoplasm - metabolism ; Dogs ; Epithelial cells ; Glycosylation ; Humans ; Kidney cells ; Membranes ; Neurons ; P branes ; Polysaccharides - chemistry ; Receptor, Nerve Growth Factor ; Receptors ; Receptors, Nerve Growth Factor - chemistry ; Receptors, Nerve Growth Factor - metabolism ; Recombinant Proteins - metabolism ; Secretion ; Serine - chemistry ; Solubility ; Structure-Activity Relationship ; Threonine - chemistry ; Transfection</subject><ispartof>The Journal of cell biology, 1997-11, Vol.139 (4), p.929-940</ispartof><rights>Copyright 1997 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Nov 17, 1997</rights><rights>1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c496t-334a61c0181ecaa721320b05b99c74a78212bfb1f22cf640e27b87923f4b9b33</citedby><cites>FETCH-LOGICAL-c496t-334a61c0181ecaa721320b05b99c74a78212bfb1f22cf640e27b87923f4b9b33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9362511$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yeaman, Charles</creatorcontrib><creatorcontrib>Le Gall, Annick H.</creatorcontrib><creatorcontrib>Baldwin, Anne N.</creatorcontrib><creatorcontrib>Monlauzeur, Laure</creatorcontrib><creatorcontrib>Le Bivic, Andre</creatorcontrib><creatorcontrib>Rodriguez-Boulan, Enrique</creatorcontrib><title>The O-Glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of transmembrane neurotrophin receptors (p75NTR) is localized to a juxtamembrane region of the extracellular domain that is rich in O-glycosylated serine/threonine residues. An internal deletion of 50 amino acids that removes this stalk domain from p75NTR causes the protein to be sorted exclusively of the basolateral plasma membrane. Basolateral sorting stalk-minus p75NTR does not occur by default, but requires sequences present in the cytoplasmic domain. The stalk domain is also required for apical secretion of a soluble form of p75NTR, providing the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well as secreted protein. However, the single N-glycan present on p75NTR is not required for apical sorting of either transmembrane or secreted forms.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Asparagine - chemistry</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Cell membranes</subject><subject>Cell Polarity</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Cytoplasm - chemistry</subject><subject>Cytoplasm - metabolism</subject><subject>Dogs</subject><subject>Epithelial cells</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Kidney cells</subject><subject>Membranes</subject><subject>Neurons</subject><subject>P branes</subject><subject>Polysaccharides - chemistry</subject><subject>Receptor, Nerve Growth Factor</subject><subject>Receptors</subject><subject>Receptors, Nerve Growth Factor - chemistry</subject><subject>Receptors, Nerve Growth Factor - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Secretion</subject><subject>Serine - chemistry</subject><subject>Solubility</subject><subject>Structure-Activity Relationship</subject><subject>Threonine - chemistry</subject><subject>Transfection</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUFvEzEQhS0EKmnhyA0kq4feNvXY3rV9QapSKBWFojZ3y3a9jcNmvbV3kcKvx1WiAj2NRu_5mxk_hN4BmQOR7HTt7ByYmvO5ouoFmkHNSSWBk5doRgiFStW0fo0Oc14TQrjg7AAdKNbQGmCGhuXK4-vqotu6mLedGf0dvh1N9xOfx40JPb7M-MY_TCEVoY0Jnw3BmQ7fxjSG_h7HFn_3U4pjisOq2G-888MYU8al-RE7k8Lv8vLb-eIrXviuy2_Qq9Z02b_d1yO0_PxpufhSXV1fXC7OrirHVTNWjHHTgCMgwTtjBAVGiSW1VcoJboSkQG1roaXUtQ0nngorhaKs5VZZxo7Qxx12mOzG3znfj8l0ekhhY9JWRxP0_0ofVvo-_tJlkFK1KICTPSDFh8nnUW9CduUC0_s4ZS0UB6glKcbjZ8Z1nFJfbissQaTk8EirdiaXYs7Jt0-bANGPMeoSoy6jNdclxuL_8O_6T-59bkV_v9PXuXz2X1gDkkrO_gCQx6JN</recordid><startdate>19971117</startdate><enddate>19971117</enddate><creator>Yeaman, Charles</creator><creator>Le Gall, Annick H.</creator><creator>Baldwin, Anne N.</creator><creator>Monlauzeur, Laure</creator><creator>Le Bivic, Andre</creator><creator>Rodriguez-Boulan, Enrique</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19971117</creationdate><title>The O-Glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells</title><author>Yeaman, Charles ; Le Gall, Annick H. ; Baldwin, Anne N. ; Monlauzeur, Laure ; Le Bivic, Andre ; Rodriguez-Boulan, Enrique</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c496t-334a61c0181ecaa721320b05b99c74a78212bfb1f22cf640e27b87923f4b9b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Asparagine - chemistry</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Cell membranes</topic><topic>Cell Polarity</topic><topic>Cells</topic><topic>Cellular biology</topic><topic>Cytoplasm - chemistry</topic><topic>Cytoplasm - metabolism</topic><topic>Dogs</topic><topic>Epithelial cells</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Kidney cells</topic><topic>Membranes</topic><topic>Neurons</topic><topic>P branes</topic><topic>Polysaccharides - chemistry</topic><topic>Receptor, Nerve Growth Factor</topic><topic>Receptors</topic><topic>Receptors, Nerve Growth Factor - chemistry</topic><topic>Receptors, Nerve Growth Factor - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Secretion</topic><topic>Serine - chemistry</topic><topic>Solubility</topic><topic>Structure-Activity Relationship</topic><topic>Threonine - chemistry</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yeaman, Charles</creatorcontrib><creatorcontrib>Le Gall, Annick H.</creatorcontrib><creatorcontrib>Baldwin, Anne N.</creatorcontrib><creatorcontrib>Monlauzeur, Laure</creatorcontrib><creatorcontrib>Le Bivic, Andre</creatorcontrib><creatorcontrib>Rodriguez-Boulan, Enrique</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yeaman, Charles</au><au>Le Gall, Annick H.</au><au>Baldwin, Anne N.</au><au>Monlauzeur, Laure</au><au>Le Bivic, Andre</au><au>Rodriguez-Boulan, Enrique</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The O-Glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1997-11-17</date><risdate>1997</risdate><volume>139</volume><issue>4</issue><spage>929</spage><epage>940</epage><pages>929-940</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Delivery of newly synthesized membrane-spanning proteins to the apical plasma membrane domain of polarized MDCK epithelial cells is dependent on yet unidentified sorting signals present in the luminal domains of these proteins. In this report we show that structural information for apical sorting of transmembrane neurotrophin receptors (p75NTR) is localized to a juxtamembrane region of the extracellular domain that is rich in O-glycosylated serine/threonine residues. An internal deletion of 50 amino acids that removes this stalk domain from p75NTR causes the protein to be sorted exclusively of the basolateral plasma membrane. Basolateral sorting stalk-minus p75NTR does not occur by default, but requires sequences present in the cytoplasmic domain. The stalk domain is also required for apical secretion of a soluble form of p75NTR, providing the first demonstration that the same domain can mediate apical sorting of both a membrane-anchored as well as secreted protein. However, the single N-glycan present on p75NTR is not required for apical sorting of either transmembrane or secreted forms.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>9362511</pmid><doi>10.1083/jcb.139.4.929</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9525 |
| ispartof | The Journal of cell biology, 1997-11, Vol.139 (4), p.929-940 |
| issn | 0021-9525 1540-8140 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2139957 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino acids Animals Asparagine - chemistry Cell Line Cell lines Cell membranes Cell Polarity Cells Cellular biology Cytoplasm - chemistry Cytoplasm - metabolism Dogs Epithelial cells Glycosylation Humans Kidney cells Membranes Neurons P branes Polysaccharides - chemistry Receptor, Nerve Growth Factor Receptors Receptors, Nerve Growth Factor - chemistry Receptors, Nerve Growth Factor - metabolism Recombinant Proteins - metabolism Secretion Serine - chemistry Solubility Structure-Activity Relationship Threonine - chemistry Transfection |
| title | The O-Glycosylated Stalk Domain Is Required for Apical Sorting of Neurotrophin Receptors in Polarized MDCK Cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T04%3A55%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20O-Glycosylated%20Stalk%20Domain%20Is%20Required%20for%20Apical%20Sorting%20of%20Neurotrophin%20Receptors%20in%20Polarized%20MDCK%20Cells&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Yeaman,%20Charles&rft.date=1997-11-17&rft.volume=139&rft.issue=4&rft.spage=929&rft.epage=940&rft.pages=929-940&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.139.4.929&rft_dat=%3Cjstor_pubme%3E1618284%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217088417&rft_id=info:pmid/9362511&rft_jstor_id=1618284&rfr_iscdi=true |