Gemin4: A Novel Component of the SMN Complex That Is Found in Both Gems and Nucleoli
The survival of motor neurons (SMN) protein, the product of the neurodegenerative disease spinal muscular atrophy (SMA) gene, is localized both in the cytoplasm and in discrete nuclear bodies called gems. In both compartments SMN is part of a large complex that contains several proteins including Ge...
Gespeichert in:
Veröffentlicht in: | The Journal of cell biology 2000-03, Vol.148 (6), p.1177-1186 |
---|---|
Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1186 |
---|---|
container_issue | 6 |
container_start_page | 1177 |
container_title | The Journal of cell biology |
container_volume | 148 |
creator | Charroux, Bernard Pellizzoni, Livio Perkinson, Robert A. Yong, Jeongsik Shevchenko, Andrej Mann, Matthias Dreyfuss, Gideon |
description | The survival of motor neurons (SMN) protein, the product of the neurodegenerative disease spinal muscular atrophy (SMA) gene, is localized both in the cytoplasm and in discrete nuclear bodies called gems. In both compartments SMN is part of a large complex that contains several proteins including Gemin2 (formerly SIP1) and the DEAD box protein Gemin3. In the cytoplasm, the SMN complex is associated with snRNP Sm core proteins and plays a critical role in spliceosomal snRNP assembly. In the nucleus, SMN is required for pre-mRNA splicing by serving in the regeneration of spliceosomes. These functions are likely impaired in cells of SMA patients because they have reduced levels of functional SMN. Here, we report the identification by nanoelectrospray mass spectrometry of a novel component of the SMN complex that we name Gemin4. Gemin4 is associated in vivo with the SMN complex through a direct interaction with Gemin3. The tight interaction of Gemin4 with Gemin3 suggests that it could serve as a cofactor of this DEAD box protein. Gemin4 also interacts directly with several of the Sm core proteins. Monoclonal antibodies against Gemin4 efficiently immunoprecipitate the spliceosomal U snRNAs U1 and U5 from Xenopus oocytes cytoplasm. Immunolocalization experiments show that Gemin4 is colocalized with SMN in the cytoplasm and in gems. Interestingly, Gemin4 is also detected in the nucleoli, suggesting that the SMN complex may also function in preribosomal RNA processing or ribosome assembly. |
doi_str_mv | 10.1083/jcb.148.6.1177 |
format | Article |
fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2174312</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1619723</jstor_id><sourcerecordid>1619723</sourcerecordid><originalsourceid>FETCH-LOGICAL-j310t-cdfe9f394f4db97cf43f7202ae131e38114fb0d990b85bfc964e0be819429e93</originalsourceid><addsrcrecordid>eNpdkDlPxDAQRi0EguVoqRCyKOiyzNjOJqZAghWXBEvB9lGOMZsoiZc4QfDvMfdRjTTz9PTNx9guwhghlkdVno1RxePJGDGKVtgIQwVBjApW2QhAYKBDEW6wTecqAFCRkutsAyESoZQ4YvNLaspWHfNTPrNPVPOpbZa2pbbn1vB-Qfz-dva-rOmZzxdpz68dv7BDW_Cy5We2X3CvcDz1i9mQ12TrcputmbR2tPM5t9j84nw-vQpu7i6vp6c3QSUR-iAvDGkjtTKqyHSUGyVNJECkhBJJxojKZFBoDVkcZibXE0WQUYxaCU1abrGTD-1yyBoqch-6S-tk2ZVN2r0kNi2Tv5e2XCQP9ikR6GtA4QWHn4LOPg7k-qQpXU51nbZkB5dEoGOpJXjw4B9Y2aFr_W9vLohDDaGH9n_H-c7xVbYH9j6AyvW2-7lPUEdCyleJtokQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217085905</pqid></control><display><type>article</type><title>Gemin4: A Novel Component of the SMN Complex That Is Found in Both Gems and Nucleoli</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Charroux, Bernard ; Pellizzoni, Livio ; Perkinson, Robert A. ; Yong, Jeongsik ; Shevchenko, Andrej ; Mann, Matthias ; Dreyfuss, Gideon</creator><creatorcontrib>Charroux, Bernard ; Pellizzoni, Livio ; Perkinson, Robert A. ; Yong, Jeongsik ; Shevchenko, Andrej ; Mann, Matthias ; Dreyfuss, Gideon</creatorcontrib><description>The survival of motor neurons (SMN) protein, the product of the neurodegenerative disease spinal muscular atrophy (SMA) gene, is localized both in the cytoplasm and in discrete nuclear bodies called gems. In both compartments SMN is part of a large complex that contains several proteins including Gemin2 (formerly SIP1) and the DEAD box protein Gemin3. In the cytoplasm, the SMN complex is associated with snRNP Sm core proteins and plays a critical role in spliceosomal snRNP assembly. In the nucleus, SMN is required for pre-mRNA splicing by serving in the regeneration of spliceosomes. These functions are likely impaired in cells of SMA patients because they have reduced levels of functional SMN. Here, we report the identification by nanoelectrospray mass spectrometry of a novel component of the SMN complex that we name Gemin4. Gemin4 is associated in vivo with the SMN complex through a direct interaction with Gemin3. The tight interaction of Gemin4 with Gemin3 suggests that it could serve as a cofactor of this DEAD box protein. Gemin4 also interacts directly with several of the Sm core proteins. Monoclonal antibodies against Gemin4 efficiently immunoprecipitate the spliceosomal U snRNAs U1 and U5 from Xenopus oocytes cytoplasm. Immunolocalization experiments show that Gemin4 is colocalized with SMN in the cytoplasm and in gems. Interestingly, Gemin4 is also detected in the nucleoli, suggesting that the SMN complex may also function in preribosomal RNA processing or ribosome assembly.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.148.6.1177</identifier><identifier>PMID: 10725331</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Animals ; Antibodies ; Antibodies, Monoclonal ; Cell nucleolus ; Cell Nucleolus - physiology ; Cell Nucleolus - ultrastructure ; Cell Nucleus - physiology ; Cell Nucleus - ultrastructure ; Cellular biology ; Cyclic AMP Response Element-Binding Protein ; Cytoplasm ; Cytoplasm - physiology ; Cytoplasm - ultrastructure ; DEAD Box Protein 20 ; DEAD-box RNA Helicases ; Female ; HeLa Cells ; Humans ; Immunoprecipitation ; Minor Histocompatibility Antigens ; Models, Molecular ; Muscular Atrophy, Spinal - genetics ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurological disorders ; Nuclear Proteins - analysis ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Oocytes ; Oocytes - physiology ; Oocytes - ultrastructure ; Original ; Proteins ; Ribonucleic acid ; Ribonucleoproteins, Small Nuclear - metabolism ; RNA ; RNA Helicases - analysis ; RNA Helicases - metabolism ; RNA-Binding Proteins ; Small nuclear ribonucleoproteins ; Small nuclear RNA ; SMN Complex Proteins ; Spinal muscular atrophy ; Xenopus laevis</subject><ispartof>The Journal of cell biology, 2000-03, Vol.148 (6), p.1177-1186</ispartof><rights>Copyright 2000 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Mar 20, 2000</rights><rights>2000 The Rockefeller University Press 2000 The Rockefeller University Press</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/PMC2174312/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174312/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,887,27931,27932,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10725331$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Charroux, Bernard</creatorcontrib><creatorcontrib>Pellizzoni, Livio</creatorcontrib><creatorcontrib>Perkinson, Robert A.</creatorcontrib><creatorcontrib>Yong, Jeongsik</creatorcontrib><creatorcontrib>Shevchenko, Andrej</creatorcontrib><creatorcontrib>Mann, Matthias</creatorcontrib><creatorcontrib>Dreyfuss, Gideon</creatorcontrib><title>Gemin4: A Novel Component of the SMN Complex That Is Found in Both Gems and Nucleoli</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The survival of motor neurons (SMN) protein, the product of the neurodegenerative disease spinal muscular atrophy (SMA) gene, is localized both in the cytoplasm and in discrete nuclear bodies called gems. In both compartments SMN is part of a large complex that contains several proteins including Gemin2 (formerly SIP1) and the DEAD box protein Gemin3. In the cytoplasm, the SMN complex is associated with snRNP Sm core proteins and plays a critical role in spliceosomal snRNP assembly. In the nucleus, SMN is required for pre-mRNA splicing by serving in the regeneration of spliceosomes. These functions are likely impaired in cells of SMA patients because they have reduced levels of functional SMN. Here, we report the identification by nanoelectrospray mass spectrometry of a novel component of the SMN complex that we name Gemin4. Gemin4 is associated in vivo with the SMN complex through a direct interaction with Gemin3. The tight interaction of Gemin4 with Gemin3 suggests that it could serve as a cofactor of this DEAD box protein. Gemin4 also interacts directly with several of the Sm core proteins. Monoclonal antibodies against Gemin4 efficiently immunoprecipitate the spliceosomal U snRNAs U1 and U5 from Xenopus oocytes cytoplasm. Immunolocalization experiments show that Gemin4 is colocalized with SMN in the cytoplasm and in gems. Interestingly, Gemin4 is also detected in the nucleoli, suggesting that the SMN complex may also function in preribosomal RNA processing or ribosome assembly.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Monoclonal</subject><subject>Cell nucleolus</subject><subject>Cell Nucleolus - physiology</subject><subject>Cell Nucleolus - ultrastructure</subject><subject>Cell Nucleus - physiology</subject><subject>Cell Nucleus - ultrastructure</subject><subject>Cellular biology</subject><subject>Cyclic AMP Response Element-Binding Protein</subject><subject>Cytoplasm</subject><subject>Cytoplasm - physiology</subject><subject>Cytoplasm - ultrastructure</subject><subject>DEAD Box Protein 20</subject><subject>DEAD-box RNA Helicases</subject><subject>Female</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Minor Histocompatibility Antigens</subject><subject>Models, Molecular</subject><subject>Muscular Atrophy, Spinal - genetics</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurological disorders</subject><subject>Nuclear Proteins - analysis</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Oocytes</subject><subject>Oocytes - physiology</subject><subject>Oocytes - ultrastructure</subject><subject>Original</subject><subject>Proteins</subject><subject>Ribonucleic acid</subject><subject>Ribonucleoproteins, Small Nuclear - metabolism</subject><subject>RNA</subject><subject>RNA Helicases - analysis</subject><subject>RNA Helicases - metabolism</subject><subject>RNA-Binding Proteins</subject><subject>Small nuclear ribonucleoproteins</subject><subject>Small nuclear RNA</subject><subject>SMN Complex Proteins</subject><subject>Spinal muscular atrophy</subject><subject>Xenopus laevis</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkDlPxDAQRi0EguVoqRCyKOiyzNjOJqZAghWXBEvB9lGOMZsoiZc4QfDvMfdRjTTz9PTNx9guwhghlkdVno1RxePJGDGKVtgIQwVBjApW2QhAYKBDEW6wTecqAFCRkutsAyESoZQ4YvNLaspWHfNTPrNPVPOpbZa2pbbn1vB-Qfz-dva-rOmZzxdpz68dv7BDW_Cy5We2X3CvcDz1i9mQ12TrcputmbR2tPM5t9j84nw-vQpu7i6vp6c3QSUR-iAvDGkjtTKqyHSUGyVNJECkhBJJxojKZFBoDVkcZibXE0WQUYxaCU1abrGTD-1yyBoqch-6S-tk2ZVN2r0kNi2Tv5e2XCQP9ikR6GtA4QWHn4LOPg7k-qQpXU51nbZkB5dEoGOpJXjw4B9Y2aFr_W9vLohDDaGH9n_H-c7xVbYH9j6AyvW2-7lPUEdCyleJtokQ</recordid><startdate>20000320</startdate><enddate>20000320</enddate><creator>Charroux, Bernard</creator><creator>Pellizzoni, Livio</creator><creator>Perkinson, Robert A.</creator><creator>Yong, Jeongsik</creator><creator>Shevchenko, Andrej</creator><creator>Mann, Matthias</creator><creator>Dreyfuss, Gideon</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>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>20000320</creationdate><title>Gemin4: A Novel Component of the SMN Complex That Is Found in Both Gems and Nucleoli</title><author>Charroux, Bernard ; Pellizzoni, Livio ; Perkinson, Robert A. ; Yong, Jeongsik ; Shevchenko, Andrej ; Mann, Matthias ; Dreyfuss, Gideon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j310t-cdfe9f394f4db97cf43f7202ae131e38114fb0d990b85bfc964e0be819429e93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Monoclonal</topic><topic>Cell nucleolus</topic><topic>Cell Nucleolus - physiology</topic><topic>Cell Nucleolus - ultrastructure</topic><topic>Cell Nucleus - physiology</topic><topic>Cell Nucleus - ultrastructure</topic><topic>Cellular biology</topic><topic>Cyclic AMP Response Element-Binding Protein</topic><topic>Cytoplasm</topic><topic>Cytoplasm - physiology</topic><topic>Cytoplasm - ultrastructure</topic><topic>DEAD Box Protein 20</topic><topic>DEAD-box RNA Helicases</topic><topic>Female</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Minor Histocompatibility Antigens</topic><topic>Models, Molecular</topic><topic>Muscular Atrophy, Spinal - genetics</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurological disorders</topic><topic>Nuclear Proteins - analysis</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Oocytes</topic><topic>Oocytes - physiology</topic><topic>Oocytes - ultrastructure</topic><topic>Original</topic><topic>Proteins</topic><topic>Ribonucleic acid</topic><topic>Ribonucleoproteins, Small Nuclear - metabolism</topic><topic>RNA</topic><topic>RNA Helicases - analysis</topic><topic>RNA Helicases - metabolism</topic><topic>RNA-Binding Proteins</topic><topic>Small nuclear ribonucleoproteins</topic><topic>Small nuclear RNA</topic><topic>SMN Complex Proteins</topic><topic>Spinal muscular atrophy</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Charroux, Bernard</creatorcontrib><creatorcontrib>Pellizzoni, Livio</creatorcontrib><creatorcontrib>Perkinson, Robert A.</creatorcontrib><creatorcontrib>Yong, Jeongsik</creatorcontrib><creatorcontrib>Shevchenko, Andrej</creatorcontrib><creatorcontrib>Mann, Matthias</creatorcontrib><creatorcontrib>Dreyfuss, Gideon</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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>Charroux, Bernard</au><au>Pellizzoni, Livio</au><au>Perkinson, Robert A.</au><au>Yong, Jeongsik</au><au>Shevchenko, Andrej</au><au>Mann, Matthias</au><au>Dreyfuss, Gideon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gemin4: A Novel Component of the SMN Complex That Is Found in Both Gems and Nucleoli</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2000-03-20</date><risdate>2000</risdate><volume>148</volume><issue>6</issue><spage>1177</spage><epage>1186</epage><pages>1177-1186</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The survival of motor neurons (SMN) protein, the product of the neurodegenerative disease spinal muscular atrophy (SMA) gene, is localized both in the cytoplasm and in discrete nuclear bodies called gems. In both compartments SMN is part of a large complex that contains several proteins including Gemin2 (formerly SIP1) and the DEAD box protein Gemin3. In the cytoplasm, the SMN complex is associated with snRNP Sm core proteins and plays a critical role in spliceosomal snRNP assembly. In the nucleus, SMN is required for pre-mRNA splicing by serving in the regeneration of spliceosomes. These functions are likely impaired in cells of SMA patients because they have reduced levels of functional SMN. Here, we report the identification by nanoelectrospray mass spectrometry of a novel component of the SMN complex that we name Gemin4. Gemin4 is associated in vivo with the SMN complex through a direct interaction with Gemin3. The tight interaction of Gemin4 with Gemin3 suggests that it could serve as a cofactor of this DEAD box protein. Gemin4 also interacts directly with several of the Sm core proteins. Monoclonal antibodies against Gemin4 efficiently immunoprecipitate the spliceosomal U snRNAs U1 and U5 from Xenopus oocytes cytoplasm. Immunolocalization experiments show that Gemin4 is colocalized with SMN in the cytoplasm and in gems. Interestingly, Gemin4 is also detected in the nucleoli, suggesting that the SMN complex may also function in preribosomal RNA processing or ribosome assembly.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>10725331</pmid><doi>10.1083/jcb.148.6.1177</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9525 |
ispartof | The Journal of cell biology, 2000-03, Vol.148 (6), p.1177-1186 |
issn | 0021-9525 1540-8140 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2174312 |
source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
subjects | Animals Antibodies Antibodies, Monoclonal Cell nucleolus Cell Nucleolus - physiology Cell Nucleolus - ultrastructure Cell Nucleus - physiology Cell Nucleus - ultrastructure Cellular biology Cyclic AMP Response Element-Binding Protein Cytoplasm Cytoplasm - physiology Cytoplasm - ultrastructure DEAD Box Protein 20 DEAD-box RNA Helicases Female HeLa Cells Humans Immunoprecipitation Minor Histocompatibility Antigens Models, Molecular Muscular Atrophy, Spinal - genetics Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurological disorders Nuclear Proteins - analysis Nuclear Proteins - genetics Nuclear Proteins - metabolism Oocytes Oocytes - physiology Oocytes - ultrastructure Original Proteins Ribonucleic acid Ribonucleoproteins, Small Nuclear - metabolism RNA RNA Helicases - analysis RNA Helicases - metabolism RNA-Binding Proteins Small nuclear ribonucleoproteins Small nuclear RNA SMN Complex Proteins Spinal muscular atrophy Xenopus laevis |
title | Gemin4: A Novel Component of the SMN Complex That Is Found in Both Gems and Nucleoli |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-05T21%3A15%3A54IST&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=Gemin4:%20A%20Novel%20Component%20of%20the%20SMN%20Complex%20That%20Is%20Found%20in%20Both%20Gems%20and%20Nucleoli&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Charroux,%20Bernard&rft.date=2000-03-20&rft.volume=148&rft.issue=6&rft.spage=1177&rft.epage=1186&rft.pages=1177-1186&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.148.6.1177&rft_dat=%3Cjstor_pubme%3E1619723%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=217085905&rft_id=info:pmid/10725331&rft_jstor_id=1619723&rfr_iscdi=true |