An essential nuclear envelope integral membrane protein, Brr6p, required for nuclear transport
Despite rapid advances in our understanding of the function of the nuclear pore complex in nuclear transport, little is known about the role the nuclear envelope itself may play in this critical process. A small number of integral membrane proteins specific to the envelope have been identified in bu...
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description | Despite rapid advances in our understanding of the function of the nuclear pore complex in nuclear transport, little is known about the role the nuclear envelope itself may play in this critical process. A small number of integral membrane proteins specific to the envelope have been identified in budding yeast, however, none has been reported to affect transport. We have identified an essential gene,
BRR6
, whose product, Brr6p, behaves like a nuclear envelope integral membrane protein. Notably, the
brr6‐1
mutant specifically affects transport of mRNA and a protein reporter containing a nuclear export signal. In addition, Brr6p depletion alters nucleoporin distribution and nuclear envelope morphology, suggesting that the protein is required for the spatial organization of nuclear pores.
BRR6
interacts genetically with a subset of nucleoporins, and Brr6‐green fluorescent protein (GFP) localizes in a punctate nuclear rim pattern, suggesting location at or near the nuclear pore. However, Brr6‐GFP fails to redistribute in a
Δnup133
mutant, distinguishing Brr6p from known proteins of the pore membrane domain. We hypothesize that Brr6p is located adjacent to the nuclear pore and interacts functionally with the pore and transport machinery. |
doi_str_mv | 10.1093/emboj/20.15.4183 |
format | Article |
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BRR6
, whose product, Brr6p, behaves like a nuclear envelope integral membrane protein. Notably, the
brr6‐1
mutant specifically affects transport of mRNA and a protein reporter containing a nuclear export signal. In addition, Brr6p depletion alters nucleoporin distribution and nuclear envelope morphology, suggesting that the protein is required for the spatial organization of nuclear pores.
BRR6
interacts genetically with a subset of nucleoporins, and Brr6‐green fluorescent protein (GFP) localizes in a punctate nuclear rim pattern, suggesting location at or near the nuclear pore. However, Brr6‐GFP fails to redistribute in a
Δnup133
mutant, distinguishing Brr6p from known proteins of the pore membrane domain. We hypothesize that Brr6p is located adjacent to the nuclear pore and interacts functionally with the pore and transport machinery.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/20.15.4183</identifier><identifier>PMID: 11483521</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Active Transport, Cell Nucleus ; BRR6 gene ; Brr6 protein ; Calcium-Binding Proteins ; Cell Nucleus - metabolism ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Green Fluorescent Proteins ; integral membrane protein ; Luminescent Proteins - genetics ; Luminescent Proteins - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; mRNA export ; Mutagenesis ; nuclear envelope ; Nuclear Envelope - metabolism ; Nuclear Pore - metabolism ; Nuclear Pore Complex Proteins ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; nuclear transport ; nucleoporins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; RNA, Fungal - metabolism ; RNA, Messenger - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Yeasts</subject><ispartof>The EMBO journal, 2001-08, Vol.20 (15), p.4183-4193</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Aug 01, 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC149179/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC149179/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11483521$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de Bruyn Kops, Anne</creatorcontrib><creatorcontrib>Guthrie, Christine</creatorcontrib><title>An essential nuclear envelope integral membrane protein, Brr6p, required for nuclear transport</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Despite rapid advances in our understanding of the function of the nuclear pore complex in nuclear transport, little is known about the role the nuclear envelope itself may play in this critical process. A small number of integral membrane proteins specific to the envelope have been identified in budding yeast, however, none has been reported to affect transport. We have identified an essential gene,
BRR6
, whose product, Brr6p, behaves like a nuclear envelope integral membrane protein. Notably, the
brr6‐1
mutant specifically affects transport of mRNA and a protein reporter containing a nuclear export signal. In addition, Brr6p depletion alters nucleoporin distribution and nuclear envelope morphology, suggesting that the protein is required for the spatial organization of nuclear pores.
BRR6
interacts genetically with a subset of nucleoporins, and Brr6‐green fluorescent protein (GFP) localizes in a punctate nuclear rim pattern, suggesting location at or near the nuclear pore. However, Brr6‐GFP fails to redistribute in a
Δnup133
mutant, distinguishing Brr6p from known proteins of the pore membrane domain. We hypothesize that Brr6p is located adjacent to the nuclear pore and interacts functionally with the pore and transport machinery.</description><subject>Active Transport, Cell Nucleus</subject><subject>BRR6 gene</subject><subject>Brr6 protein</subject><subject>Calcium-Binding Proteins</subject><subject>Cell Nucleus - metabolism</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Green Fluorescent Proteins</subject><subject>integral membrane protein</subject><subject>Luminescent Proteins - genetics</subject><subject>Luminescent Proteins - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>mRNA export</subject><subject>Mutagenesis</subject><subject>nuclear envelope</subject><subject>Nuclear Envelope - metabolism</subject><subject>Nuclear Pore - metabolism</subject><subject>Nuclear Pore Complex Proteins</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>nuclear transport</subject><subject>nucleoporins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RNA, Fungal - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Yeasts</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kc9PFTEQxxujkSd692Q2Hjix0N_dHjwAQYVgvHC26e5On33ZbZd2F8N_b58PAU04NTPz_cx8p4PQe4KPCNbsGMY2bo5picQRJw17gVaES1xTrMRLtMJUkrrk9R56k_MGYywaRV6jPUJ4wwQlK_TjJFSQM4TZ26EKSzeATRWEWxjiBJUPM6xTqYxlVLIBqinFGXw4rE5TktNhleBm8Qn6ysX0wM9FmqeY5rfolbNDhnf37z66_nx-ffa1vvr-5eLs5KqeGGeituCAaGg5JU4q5ToqgbXOMd0pSdueMu5Yr2XbgXTWNT3nWtiSUFRhx9g--rRrOy3tCH1X1immzZT8aNOdidabfyvB_zTreGsI10Tpwh_c8yneLJBnM_rcwTCUjeOSTdFg2sjtoI__CTdxSaGsZogWVHLNtt0-PHXzYOPvrxeB3gl--QHuHuvYbK9q_lzV0BIJs72qOf92eqlEaU1EYcmOzQULa0hPHDzDs99gX6mD</recordid><startdate>20010801</startdate><enddate>20010801</enddate><creator>de Bruyn Kops, Anne</creator><creator>Guthrie, Christine</creator><general>Nature Publishing Group UK</general><general>John Wiley & Sons, Ltd</general><general>Springer Nature B.V</general><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20010801</creationdate><title>An essential nuclear envelope integral membrane protein, Brr6p, required for nuclear transport</title><author>de Bruyn Kops, Anne ; Guthrie, Christine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p3435-aefe19eb421f677fc26e3bff39c762bd234f3d96bce6faf8d4495ad967270f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Active Transport, Cell Nucleus</topic><topic>BRR6 gene</topic><topic>Brr6 protein</topic><topic>Calcium-Binding Proteins</topic><topic>Cell Nucleus - metabolism</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Green Fluorescent Proteins</topic><topic>integral membrane protein</topic><topic>Luminescent Proteins - genetics</topic><topic>Luminescent Proteins - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membranes</topic><topic>mRNA export</topic><topic>Mutagenesis</topic><topic>nuclear envelope</topic><topic>Nuclear Envelope - metabolism</topic><topic>Nuclear Pore - metabolism</topic><topic>Nuclear Pore Complex Proteins</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>nuclear transport</topic><topic>nucleoporins</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RNA, Fungal - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>de Bruyn Kops, Anne</creatorcontrib><creatorcontrib>Guthrie, Christine</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de Bruyn Kops, Anne</au><au>Guthrie, Christine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An essential nuclear envelope integral membrane protein, Brr6p, required for nuclear transport</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2001-08-01</date><risdate>2001</risdate><volume>20</volume><issue>15</issue><spage>4183</spage><epage>4193</epage><pages>4183-4193</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Despite rapid advances in our understanding of the function of the nuclear pore complex in nuclear transport, little is known about the role the nuclear envelope itself may play in this critical process. A small number of integral membrane proteins specific to the envelope have been identified in budding yeast, however, none has been reported to affect transport. We have identified an essential gene,
BRR6
, whose product, Brr6p, behaves like a nuclear envelope integral membrane protein. Notably, the
brr6‐1
mutant specifically affects transport of mRNA and a protein reporter containing a nuclear export signal. In addition, Brr6p depletion alters nucleoporin distribution and nuclear envelope morphology, suggesting that the protein is required for the spatial organization of nuclear pores.
BRR6
interacts genetically with a subset of nucleoporins, and Brr6‐green fluorescent protein (GFP) localizes in a punctate nuclear rim pattern, suggesting location at or near the nuclear pore. However, Brr6‐GFP fails to redistribute in a
Δnup133
mutant, distinguishing Brr6p from known proteins of the pore membrane domain. We hypothesize that Brr6p is located adjacent to the nuclear pore and interacts functionally with the pore and transport machinery.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>11483521</pmid><doi>10.1093/emboj/20.15.4183</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Active Transport, Cell Nucleus BRR6 gene Brr6 protein Calcium-Binding Proteins Cell Nucleus - metabolism Fungal Proteins - genetics Fungal Proteins - metabolism Green Fluorescent Proteins integral membrane protein Luminescent Proteins - genetics Luminescent Proteins - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Membranes mRNA export Mutagenesis nuclear envelope Nuclear Envelope - metabolism Nuclear Pore - metabolism Nuclear Pore Complex Proteins Nuclear Proteins - genetics Nuclear Proteins - metabolism nuclear transport nucleoporins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA, Fungal - metabolism RNA, Messenger - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Yeasts |
title | An essential nuclear envelope integral membrane protein, Brr6p, required for nuclear transport |
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