Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform
The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer pre...
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| Veröffentlicht in: | Cell 2016-11, Vol.167 (5), p.1215-1228.e25 |
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| creator | Fernandez-Martinez, Javier Kim, Seung Joong Shi, Yi Upla, Paula Pellarin, Riccardo Gagnon, Michael Chemmama, Ilan E. Wang, Junjie Nudelman, Ilona Zhang, Wenzhu Williams, Rosemary Rice, William J. Stokes, David L. Zenklusen, Daniel Chait, Brian T. Sali, Andrej Rout, Michael P. |
| description | The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer precision. The complex consists of two compositionally identical multiprotein subunits that adopt different configurations. The Nup82 complex fits into the NPC through the outer ring Nup84 complex. Our map shows that this entire 14-MDa Nup82-Nup84 complex assembly positions the cytoplasmic mRNA export factor docking sites and messenger ribonucleoprotein (mRNP) remodeling machinery right over the NPC’s central channel rather than on distal cytoplasmic filaments, as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC.
[Display omitted]
•Integrative structure at 9 Å precision of the endogenous Nup82 holo-complex•Molecular architecture of the conserved 1.8-MDa cytoplasmic mRNA export platform•Structural framework to understand the mRNP remodeling and export processes•mRNP remodeling machinery is positioned over the NPC’s central channel, not in filaments
mRNAs escape the nucleus with help from a nuclear pore subcomplex that sits directly over the transport channel in the cytoplasm. |
| doi_str_mv | 10.1016/j.cell.2016.10.028 |
| format | Article |
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[Display omitted]
•Integrative structure at 9 Å precision of the endogenous Nup82 holo-complex•Molecular architecture of the conserved 1.8-MDa cytoplasmic mRNA export platform•Structural framework to understand the mRNP remodeling and export processes•mRNP remodeling machinery is positioned over the NPC’s central channel, not in filaments
mRNAs escape the nucleus with help from a nuclear pore subcomplex that sits directly over the transport channel in the cytoplasm.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/j.cell.2016.10.028</identifier><identifier>PMID: 27839866</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Active Transport, Cell Nucleus ; computational structural biology ; cross-linking and mass spectrometry ; electron microscopy ; Fungal Proteins ; integrative structure determination ; messenger RNA ; mRNA export ; mRNP remodeling ; Nuclear Pore - chemistry ; nuclear pore complex ; Nuclear Pore Complex Proteins - chemistry ; Nuclear Pore Complex Proteins - ultrastructure ; nucleoporins ; Nup82 complex ; Nup84 complex ; ribonucleoproteins ; RNA transport ; RNA, Messenger ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; Saccharomyces cerevisiae Proteins - ultrastructure ; small-angle X-ray scattering ; Yeasts - metabolism</subject><ispartof>Cell, 2016-11, Vol.167 (5), p.1215-1228.e25</ispartof><rights>2016 Elsevier Inc.</rights><rights>Copyright © 2016 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c603t-3923ff3afb76e09aa35461ab3dd55b08ba523e3ab08ac3459e800c16c05a89763</citedby><cites>FETCH-LOGICAL-c603t-3923ff3afb76e09aa35461ab3dd55b08ba523e3ab08ac3459e800c16c05a89763</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0092867416314489$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27839866$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fernandez-Martinez, Javier</creatorcontrib><creatorcontrib>Kim, Seung Joong</creatorcontrib><creatorcontrib>Shi, Yi</creatorcontrib><creatorcontrib>Upla, Paula</creatorcontrib><creatorcontrib>Pellarin, Riccardo</creatorcontrib><creatorcontrib>Gagnon, Michael</creatorcontrib><creatorcontrib>Chemmama, Ilan E.</creatorcontrib><creatorcontrib>Wang, Junjie</creatorcontrib><creatorcontrib>Nudelman, Ilona</creatorcontrib><creatorcontrib>Zhang, Wenzhu</creatorcontrib><creatorcontrib>Williams, Rosemary</creatorcontrib><creatorcontrib>Rice, William J.</creatorcontrib><creatorcontrib>Stokes, David L.</creatorcontrib><creatorcontrib>Zenklusen, Daniel</creatorcontrib><creatorcontrib>Chait, Brian T.</creatorcontrib><creatorcontrib>Sali, Andrej</creatorcontrib><creatorcontrib>Rout, Michael P.</creatorcontrib><title>Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform</title><title>Cell</title><addtitle>Cell</addtitle><description>The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer precision. The complex consists of two compositionally identical multiprotein subunits that adopt different configurations. The Nup82 complex fits into the NPC through the outer ring Nup84 complex. Our map shows that this entire 14-MDa Nup82-Nup84 complex assembly positions the cytoplasmic mRNA export factor docking sites and messenger ribonucleoprotein (mRNP) remodeling machinery right over the NPC’s central channel rather than on distal cytoplasmic filaments, as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC.
[Display omitted]
•Integrative structure at 9 Å precision of the endogenous Nup82 holo-complex•Molecular architecture of the conserved 1.8-MDa cytoplasmic mRNA export platform•Structural framework to understand the mRNP remodeling and export processes•mRNP remodeling machinery is positioned over the NPC’s central channel, not in filaments
mRNAs escape the nucleus with help from a nuclear pore subcomplex that sits directly over the transport channel in the cytoplasm.</description><subject>Active Transport, Cell Nucleus</subject><subject>computational structural biology</subject><subject>cross-linking and mass spectrometry</subject><subject>electron microscopy</subject><subject>Fungal Proteins</subject><subject>integrative structure determination</subject><subject>messenger RNA</subject><subject>mRNA export</subject><subject>mRNP remodeling</subject><subject>Nuclear Pore - chemistry</subject><subject>nuclear pore complex</subject><subject>Nuclear Pore Complex Proteins - chemistry</subject><subject>Nuclear Pore Complex Proteins - ultrastructure</subject><subject>nucleoporins</subject><subject>Nup82 complex</subject><subject>Nup84 complex</subject><subject>ribonucleoproteins</subject><subject>RNA transport</subject><subject>RNA, Messenger</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - ultrastructure</subject><subject>small-angle X-ray scattering</subject><subject>Yeasts - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUcFu1TAQtBCIPgo_wAH5yCWvazt2EgkhVU8tVKpKReFsOc6G-imJg-1U7d_j6JUKLqA97Go9M1rPEPKWwZYBUyf7rcVh2PI858UWeP2MbBg0VVGyij8nG4CGF7WqyiPyKsY9ANRSypfkiFe1aGqlNuTmJoXFpiUgNVNHz5fJJucn6nuabpFeLXZAE-i1z4CdH-cB7-nuIfl5MHF0lo5fr07p2f3sQ6LXg0m9D-Nr8qI3Q8Q3j_2YfD8_-7b7XFx--XSxO70srAKRCtFw0ffC9G2lEBpjhCwVM63oOilbqFsjuUBh8misKGWDNYBlyoI0dVMpcUw-HnTnpR2xszilYAY9Bzea8KC9cfrvl8nd6h_-TksmsmdlFnj_KBD8zwVj0qOLq6dmQr9EzbNjQgrI9T8oy4YyBhVbz-IHqA0-xoD900UM9Bqc3uuVqdfg1l0OLpPe_fmXJ8rvpDLgwwGA2dE7h0FH63Cy2LmANunOu3_p_wJJXKoh</recordid><startdate>20161117</startdate><enddate>20161117</enddate><creator>Fernandez-Martinez, Javier</creator><creator>Kim, Seung Joong</creator><creator>Shi, Yi</creator><creator>Upla, Paula</creator><creator>Pellarin, Riccardo</creator><creator>Gagnon, Michael</creator><creator>Chemmama, Ilan E.</creator><creator>Wang, Junjie</creator><creator>Nudelman, Ilona</creator><creator>Zhang, Wenzhu</creator><creator>Williams, Rosemary</creator><creator>Rice, William J.</creator><creator>Stokes, David L.</creator><creator>Zenklusen, Daniel</creator><creator>Chait, Brian T.</creator><creator>Sali, Andrej</creator><creator>Rout, Michael P.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20161117</creationdate><title>Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform</title><author>Fernandez-Martinez, Javier ; Kim, Seung Joong ; Shi, Yi ; Upla, Paula ; Pellarin, Riccardo ; Gagnon, Michael ; Chemmama, Ilan E. ; Wang, Junjie ; Nudelman, Ilona ; Zhang, Wenzhu ; Williams, Rosemary ; Rice, William J. ; Stokes, David L. ; Zenklusen, Daniel ; Chait, Brian T. ; Sali, Andrej ; Rout, Michael P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c603t-3923ff3afb76e09aa35461ab3dd55b08ba523e3ab08ac3459e800c16c05a89763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Active Transport, Cell Nucleus</topic><topic>computational structural biology</topic><topic>cross-linking and mass spectrometry</topic><topic>electron microscopy</topic><topic>Fungal Proteins</topic><topic>integrative structure determination</topic><topic>messenger RNA</topic><topic>mRNA export</topic><topic>mRNP remodeling</topic><topic>Nuclear Pore - chemistry</topic><topic>nuclear pore complex</topic><topic>Nuclear Pore Complex Proteins - chemistry</topic><topic>Nuclear Pore Complex Proteins - ultrastructure</topic><topic>nucleoporins</topic><topic>Nup82 complex</topic><topic>Nup84 complex</topic><topic>ribonucleoproteins</topic><topic>RNA transport</topic><topic>RNA, Messenger</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - ultrastructure</topic><topic>small-angle X-ray scattering</topic><topic>Yeasts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fernandez-Martinez, Javier</creatorcontrib><creatorcontrib>Kim, Seung Joong</creatorcontrib><creatorcontrib>Shi, Yi</creatorcontrib><creatorcontrib>Upla, Paula</creatorcontrib><creatorcontrib>Pellarin, Riccardo</creatorcontrib><creatorcontrib>Gagnon, Michael</creatorcontrib><creatorcontrib>Chemmama, Ilan E.</creatorcontrib><creatorcontrib>Wang, Junjie</creatorcontrib><creatorcontrib>Nudelman, Ilona</creatorcontrib><creatorcontrib>Zhang, Wenzhu</creatorcontrib><creatorcontrib>Williams, Rosemary</creatorcontrib><creatorcontrib>Rice, William J.</creatorcontrib><creatorcontrib>Stokes, David L.</creatorcontrib><creatorcontrib>Zenklusen, Daniel</creatorcontrib><creatorcontrib>Chait, Brian T.</creatorcontrib><creatorcontrib>Sali, Andrej</creatorcontrib><creatorcontrib>Rout, Michael P.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fernandez-Martinez, Javier</au><au>Kim, Seung Joong</au><au>Shi, Yi</au><au>Upla, Paula</au><au>Pellarin, Riccardo</au><au>Gagnon, Michael</au><au>Chemmama, Ilan E.</au><au>Wang, Junjie</au><au>Nudelman, Ilona</au><au>Zhang, Wenzhu</au><au>Williams, Rosemary</au><au>Rice, William J.</au><au>Stokes, David L.</au><au>Zenklusen, Daniel</au><au>Chait, Brian T.</au><au>Sali, Andrej</au><au>Rout, Michael P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2016-11-17</date><risdate>2016</risdate><volume>167</volume><issue>5</issue><spage>1215</spage><epage>1228.e25</epage><pages>1215-1228.e25</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer precision. The complex consists of two compositionally identical multiprotein subunits that adopt different configurations. The Nup82 complex fits into the NPC through the outer ring Nup84 complex. Our map shows that this entire 14-MDa Nup82-Nup84 complex assembly positions the cytoplasmic mRNA export factor docking sites and messenger ribonucleoprotein (mRNP) remodeling machinery right over the NPC’s central channel rather than on distal cytoplasmic filaments, as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC.
[Display omitted]
•Integrative structure at 9 Å precision of the endogenous Nup82 holo-complex•Molecular architecture of the conserved 1.8-MDa cytoplasmic mRNA export platform•Structural framework to understand the mRNP remodeling and export processes•mRNP remodeling machinery is positioned over the NPC’s central channel, not in filaments
mRNAs escape the nucleus with help from a nuclear pore subcomplex that sits directly over the transport channel in the cytoplasm.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>27839866</pmid><doi>10.1016/j.cell.2016.10.028</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Active Transport, Cell Nucleus computational structural biology cross-linking and mass spectrometry electron microscopy Fungal Proteins integrative structure determination messenger RNA mRNA export mRNP remodeling Nuclear Pore - chemistry nuclear pore complex Nuclear Pore Complex Proteins - chemistry Nuclear Pore Complex Proteins - ultrastructure nucleoporins Nup82 complex Nup84 complex ribonucleoproteins RNA transport RNA, Messenger Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure small-angle X-ray scattering Yeasts - metabolism |
| title | Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform |
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