Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
The conserved oligomeric Golgi (COG) complex is an evolutionarily conserved multi-subunit protein complex that regulates membrane trafficking in eukaryotic cells. In this work we used short interfering RNA strategy to achieve an efficient knockdown (KD) of Cog3p in HeLa cells. For the first time, we...
Gespeichert in:
| Veröffentlicht in: | The Journal of cell biology 2005-02, Vol.168 (5), p.747-759 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 759 |
|---|---|
| container_issue | 5 |
| container_start_page | 747 |
| container_title | The Journal of cell biology |
| container_volume | 168 |
| creator | Zolov, Sergey N Lupashin, Vladimir V |
| description | The conserved oligomeric Golgi (COG) complex is an evolutionarily conserved multi-subunit protein complex that regulates membrane trafficking in eukaryotic cells. In this work we used short interfering RNA strategy to achieve an efficient knockdown (KD) of Cog3p in HeLa cells. For the first time, we have demonstrated that Cog3p depletion is accompanied by reduction in Cog1, 2, and 4 protein levels and by accumulation of COG complex-dependent (CCD) vesicles carrying v-SNAREs GS15 and GS28 and cis-Golgi glycoprotein GPP130. Some of these CCD vesicles appeared to be vesicular coat complex I (COPI) coated. A prolonged block in CCD vesicles tethering is accompanied by extensive fragmentation of the Golgi ribbon. Fragmented Golgi membranes maintained their juxtanuclear localization, cisternal organization and are competent for the anterograde trafficking of vesicular stomatitis virus G protein to the plasma membrane. In a contrast, Cog3p KD resulted in inhibition of retrograde trafficking of the Shiga toxin. Furthermore, the mammalian COG complex physically interacts with GS28 and COPI and specifically binds to isolated CCD vesicles. |
| doi_str_mv | 10.1083/jcb.200412003 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2171815</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3658008</jstor_id><sourcerecordid>3658008</sourcerecordid><originalsourceid>FETCH-LOGICAL-c523t-508034621e4d99299a59040479e1f6b0ed33c9606146a9aa5ff4734e287d29073</originalsourceid><addsrcrecordid>eNpdkU1vEzEQhi1ERdPAkRsCqwduW8afu74goQjaSpGQgJ4txzu7ON2sg72pxL-vQ6JAudiHefTqmXkJec3gikEjPqz96ooDSFYe8YzMmJJQNUzCczID4KwyiqtzcpHzGgpWS_GCnDNV84YZNSPfFrEXW9ridsApxJGuhujvM33AHPyA1Qbb4CZs6XUc-kATTin2ybVIp-S6Lvj7MPY0jPQGl456HIb8kpx1bsj46vjPyd2Xzz8WN9Xy6_Xt4tOy8oqLqVLQgJCaM5StMdwYpwzIYmiQdXoF2ArhjQbNpHbGOdV1shYSeVO33EAt5uTjIXe7WxVNj2NRGuw2hY1Lv210wT6djOGn7eOD5axmDVMl4P0xIMVfO8yT3YS8X8GNGHfZ6np_Lq0LePkfuI67NJbl_mSBMVIWqDpAPsWcE3YnEwZ2X5UtVdlTVYV_-6_-X_rYTQHeHIB1nmI6zYVWDZS4OXl3GHcuWtenkO3ddw5MQPFRulbiEeokoI8</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217109944</pqid></control><display><type>article</type><title>Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Zolov, Sergey N ; Lupashin, Vladimir V</creator><creatorcontrib>Zolov, Sergey N ; Lupashin, Vladimir V</creatorcontrib><description>The conserved oligomeric Golgi (COG) complex is an evolutionarily conserved multi-subunit protein complex that regulates membrane trafficking in eukaryotic cells. In this work we used short interfering RNA strategy to achieve an efficient knockdown (KD) of Cog3p in HeLa cells. For the first time, we have demonstrated that Cog3p depletion is accompanied by reduction in Cog1, 2, and 4 protein levels and by accumulation of COG complex-dependent (CCD) vesicles carrying v-SNAREs GS15 and GS28 and cis-Golgi glycoprotein GPP130. Some of these CCD vesicles appeared to be vesicular coat complex I (COPI) coated. A prolonged block in CCD vesicles tethering is accompanied by extensive fragmentation of the Golgi ribbon. Fragmented Golgi membranes maintained their juxtanuclear localization, cisternal organization and are competent for the anterograde trafficking of vesicular stomatitis virus G protein to the plasma membrane. In a contrast, Cog3p KD resulted in inhibition of retrograde trafficking of the Shiga toxin. Furthermore, the mammalian COG complex physically interacts with GS28 and COPI and specifically binds to isolated CCD vesicles.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200412003</identifier><identifier>PMID: 15728195</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adaptor Proteins, Vesicular Transport - deficiency ; Adaptor Proteins, Vesicular Transport - metabolism ; Animals ; Antibodies ; Cell membranes ; Cells ; Cellular biology ; CHO cells ; Coat Protein Complex I - metabolism ; Cogs ; Cytoplasmic Vesicles - metabolism ; Cytoplasmic Vesicles - ultrastructure ; Endoplasmic Reticulum - ultrastructure ; Golgi apparatus ; Golgi Apparatus - metabolism ; Golgi Apparatus - ultrastructure ; HeLa Cells ; Humans ; Membrane Glycoproteins - metabolism ; Mice ; Microscopy, Electron ; P branes ; Phosphoproteins - metabolism ; Protein Transport - physiology ; Proteins ; Saccharomyces cerevisiae Proteins ; Shiga Toxin - metabolism ; Small interfering RNA ; SNARE Proteins ; Transfection ; Vesicular Transport Proteins - metabolism ; Yeasts</subject><ispartof>The Journal of cell biology, 2005-02, Vol.168 (5), p.747-759</ispartof><rights>Copyright 2005 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Feb 28, 2005</rights><rights>Copyright © 2005, The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-508034621e4d99299a59040479e1f6b0ed33c9606146a9aa5ff4734e287d29073</citedby><cites>FETCH-LOGICAL-c523t-508034621e4d99299a59040479e1f6b0ed33c9606146a9aa5ff4734e287d29073</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,778,782,883,27911,27912</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15728195$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zolov, Sergey N</creatorcontrib><creatorcontrib>Lupashin, Vladimir V</creatorcontrib><title>Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The conserved oligomeric Golgi (COG) complex is an evolutionarily conserved multi-subunit protein complex that regulates membrane trafficking in eukaryotic cells. In this work we used short interfering RNA strategy to achieve an efficient knockdown (KD) of Cog3p in HeLa cells. For the first time, we have demonstrated that Cog3p depletion is accompanied by reduction in Cog1, 2, and 4 protein levels and by accumulation of COG complex-dependent (CCD) vesicles carrying v-SNAREs GS15 and GS28 and cis-Golgi glycoprotein GPP130. Some of these CCD vesicles appeared to be vesicular coat complex I (COPI) coated. A prolonged block in CCD vesicles tethering is accompanied by extensive fragmentation of the Golgi ribbon. Fragmented Golgi membranes maintained their juxtanuclear localization, cisternal organization and are competent for the anterograde trafficking of vesicular stomatitis virus G protein to the plasma membrane. In a contrast, Cog3p KD resulted in inhibition of retrograde trafficking of the Shiga toxin. Furthermore, the mammalian COG complex physically interacts with GS28 and COPI and specifically binds to isolated CCD vesicles.</description><subject>Adaptor Proteins, Vesicular Transport - deficiency</subject><subject>Adaptor Proteins, Vesicular Transport - metabolism</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Cell membranes</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>CHO cells</subject><subject>Coat Protein Complex I - metabolism</subject><subject>Cogs</subject><subject>Cytoplasmic Vesicles - metabolism</subject><subject>Cytoplasmic Vesicles - ultrastructure</subject><subject>Endoplasmic Reticulum - ultrastructure</subject><subject>Golgi apparatus</subject><subject>Golgi Apparatus - metabolism</subject><subject>Golgi Apparatus - ultrastructure</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mice</subject><subject>Microscopy, Electron</subject><subject>P branes</subject><subject>Phosphoproteins - metabolism</subject><subject>Protein Transport - physiology</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Shiga Toxin - metabolism</subject><subject>Small interfering RNA</subject><subject>SNARE Proteins</subject><subject>Transfection</subject><subject>Vesicular Transport Proteins - metabolism</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1vEzEQhi1ERdPAkRsCqwduW8afu74goQjaSpGQgJ4txzu7ON2sg72pxL-vQ6JAudiHefTqmXkJec3gikEjPqz96ooDSFYe8YzMmJJQNUzCczID4KwyiqtzcpHzGgpWS_GCnDNV84YZNSPfFrEXW9ridsApxJGuhujvM33AHPyA1Qbb4CZs6XUc-kATTin2ybVIp-S6Lvj7MPY0jPQGl456HIb8kpx1bsj46vjPyd2Xzz8WN9Xy6_Xt4tOy8oqLqVLQgJCaM5StMdwYpwzIYmiQdXoF2ArhjQbNpHbGOdV1shYSeVO33EAt5uTjIXe7WxVNj2NRGuw2hY1Lv210wT6djOGn7eOD5axmDVMl4P0xIMVfO8yT3YS8X8GNGHfZ6np_Lq0LePkfuI67NJbl_mSBMVIWqDpAPsWcE3YnEwZ2X5UtVdlTVYV_-6_-X_rYTQHeHIB1nmI6zYVWDZS4OXl3GHcuWtenkO3ddw5MQPFRulbiEeokoI8</recordid><startdate>20050228</startdate><enddate>20050228</enddate><creator>Zolov, Sergey N</creator><creator>Lupashin, Vladimir V</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</scope><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>20050228</creationdate><title>Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells</title><author>Zolov, Sergey N ; Lupashin, Vladimir V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-508034621e4d99299a59040479e1f6b0ed33c9606146a9aa5ff4734e287d29073</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adaptor Proteins, Vesicular Transport - deficiency</topic><topic>Adaptor Proteins, Vesicular Transport - metabolism</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Cell membranes</topic><topic>Cells</topic><topic>Cellular biology</topic><topic>CHO cells</topic><topic>Coat Protein Complex I - metabolism</topic><topic>Cogs</topic><topic>Cytoplasmic Vesicles - metabolism</topic><topic>Cytoplasmic Vesicles - ultrastructure</topic><topic>Endoplasmic Reticulum - ultrastructure</topic><topic>Golgi apparatus</topic><topic>Golgi Apparatus - metabolism</topic><topic>Golgi Apparatus - ultrastructure</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Mice</topic><topic>Microscopy, Electron</topic><topic>P branes</topic><topic>Phosphoproteins - metabolism</topic><topic>Protein Transport - physiology</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Shiga Toxin - metabolism</topic><topic>Small interfering RNA</topic><topic>SNARE Proteins</topic><topic>Transfection</topic><topic>Vesicular Transport Proteins - metabolism</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zolov, Sergey N</creatorcontrib><creatorcontrib>Lupashin, Vladimir V</creatorcontrib><collection>AGRIS</collection><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>Zolov, Sergey N</au><au>Lupashin, Vladimir V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2005-02-28</date><risdate>2005</risdate><volume>168</volume><issue>5</issue><spage>747</spage><epage>759</epage><pages>747-759</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The conserved oligomeric Golgi (COG) complex is an evolutionarily conserved multi-subunit protein complex that regulates membrane trafficking in eukaryotic cells. In this work we used short interfering RNA strategy to achieve an efficient knockdown (KD) of Cog3p in HeLa cells. For the first time, we have demonstrated that Cog3p depletion is accompanied by reduction in Cog1, 2, and 4 protein levels and by accumulation of COG complex-dependent (CCD) vesicles carrying v-SNAREs GS15 and GS28 and cis-Golgi glycoprotein GPP130. Some of these CCD vesicles appeared to be vesicular coat complex I (COPI) coated. A prolonged block in CCD vesicles tethering is accompanied by extensive fragmentation of the Golgi ribbon. Fragmented Golgi membranes maintained their juxtanuclear localization, cisternal organization and are competent for the anterograde trafficking of vesicular stomatitis virus G protein to the plasma membrane. In a contrast, Cog3p KD resulted in inhibition of retrograde trafficking of the Shiga toxin. Furthermore, the mammalian COG complex physically interacts with GS28 and COPI and specifically binds to isolated CCD vesicles.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>15728195</pmid><doi>10.1083/jcb.200412003</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9525 |
| ispartof | The Journal of cell biology, 2005-02, Vol.168 (5), p.747-759 |
| issn | 0021-9525 1540-8140 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2171815 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adaptor Proteins, Vesicular Transport - deficiency Adaptor Proteins, Vesicular Transport - metabolism Animals Antibodies Cell membranes Cells Cellular biology CHO cells Coat Protein Complex I - metabolism Cogs Cytoplasmic Vesicles - metabolism Cytoplasmic Vesicles - ultrastructure Endoplasmic Reticulum - ultrastructure Golgi apparatus Golgi Apparatus - metabolism Golgi Apparatus - ultrastructure HeLa Cells Humans Membrane Glycoproteins - metabolism Mice Microscopy, Electron P branes Phosphoproteins - metabolism Protein Transport - physiology Proteins Saccharomyces cerevisiae Proteins Shiga Toxin - metabolism Small interfering RNA SNARE Proteins Transfection Vesicular Transport Proteins - metabolism Yeasts |
| title | Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T20%3A49%3A47IST&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=Cog3p%20depletion%20blocks%20vesicle-mediated%20Golgi%20retrograde%20trafficking%20in%20HeLa%20cells&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Zolov,%20Sergey%20N&rft.date=2005-02-28&rft.volume=168&rft.issue=5&rft.spage=747&rft.epage=759&rft.pages=747-759&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.200412003&rft_dat=%3Cjstor_pubme%3E3658008%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=217109944&rft_id=info:pmid/15728195&rft_jstor_id=3658008&rfr_iscdi=true |