Nucleolin: a multiFACeTed protein
Nucleolin is an abundant, ubiquitously expressed protein that is found in various cell compartments, especially in the nucleolus, of which it is a major component. This multifunctional protein has been described as being a part of many pathways, from interactions with viruses at the cellular membran...
Gespeichert in:
Veröffentlicht in: | Trends in cell biology 2007-02, Vol.17 (2), p.80-86 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 86 |
---|---|
container_issue | 2 |
container_start_page | 80 |
container_title | Trends in cell biology |
container_volume | 17 |
creator | Mongelard, Fabien Bouvet, Philippe |
description | Nucleolin is an abundant, ubiquitously expressed protein that is found in various cell compartments, especially in the nucleolus, of which it is a major component. This multifunctional protein has been described as being a part of many pathways, from interactions with viruses at the cellular membrane to essential processing of the ribosomal RNA in the nucleolus. However, most of the molecular details of these different functions are not understood. Here, we focus on the role of nucleolin in transcription, especially some recent findings describing the protein as a histone chaperone [with functional similarity to the facilitates chromatin transcription (FACT) complex] and a chromatin co-remodeler. These new properties could help reconcile discrepancies in the literature regarding the role of nucleolin in transcription. |
doi_str_mv | 10.1016/j.tcb.2006.11.010 |
format | Article |
fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_00337685v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0962892406003370</els_id><sourcerecordid>68988536</sourcerecordid><originalsourceid>FETCH-LOGICAL-c471t-f9cde1728e1090332907b73486fc0db25be2509cd68966a9c4b24dcf828502ac3</originalsourceid><addsrcrecordid>eNqFkU2L1EAQhhtR3NnVH-BFxovgIbGqO-kPF4RhcF1h0IPruUg6Fewxk6zpZGH_vZ2dQcGDnhqKp94unleIFwg5Auq3-3zydS4BdI6YA8IjsUJrXKbA2sdiBU7LzDpZnInzGPcAYCSqp-IMDZamBLUSrz7PvuOhC_27dbU-zN0UrjZbvuFmfTsOE4f-mXjSVl3k56f3Qny7-nCzvc52Xz5-2m52mS8MTlnrfMNopGUEB0pJB6Y2qrC69dDUsqxZlpAgbZ3WlfNFLYvGt1baEmTl1YV4c8z9XnV0O4ZDNd7TUAW63uxomUFKNdqWd5jY10c23fhz5jjRIUTPXVf1PMyR0h_Wlkr_F0RnC51CE4hH0I9DjCO3v09AoEU27SnJpkU2IVKSnXZensLn-sDNn42T3QRcHgFO3u4CjxR94N5zE0b2EzVD-Gf8-7-2faop-Kr7wfcc98M89qkQQoqSgL4ubS9lg34wBeoXnGSgMg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19846768</pqid></control><display><type>article</type><title>Nucleolin: a multiFACeTed protein</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Mongelard, Fabien ; Bouvet, Philippe</creator><creatorcontrib>Mongelard, Fabien ; Bouvet, Philippe</creatorcontrib><description>Nucleolin is an abundant, ubiquitously expressed protein that is found in various cell compartments, especially in the nucleolus, of which it is a major component. This multifunctional protein has been described as being a part of many pathways, from interactions with viruses at the cellular membrane to essential processing of the ribosomal RNA in the nucleolus. However, most of the molecular details of these different functions are not understood. Here, we focus on the role of nucleolin in transcription, especially some recent findings describing the protein as a histone chaperone [with functional similarity to the facilitates chromatin transcription (FACT) complex] and a chromatin co-remodeler. These new properties could help reconcile discrepancies in the literature regarding the role of nucleolin in transcription.</description><identifier>ISSN: 0962-8924</identifier><identifier>EISSN: 1879-3088</identifier><identifier>DOI: 10.1016/j.tcb.2006.11.010</identifier><identifier>PMID: 17157503</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Cell Compartmentation ; Cell Nucleolus - metabolism ; Cell Nucleolus - ultrastructure ; Chromatin - chemistry ; Chromatin - genetics ; Chromatin - ultrastructure ; DNA, Ribosomal - metabolism ; DNA-Binding Proteins - physiology ; DNA-Directed RNA Polymerases - metabolism ; Eukaryotic Cells - metabolism ; Eukaryotic Cells - ultrastructure ; Fungal Proteins - physiology ; Gene Expression Regulation ; High Mobility Group Proteins - physiology ; Histones - physiology ; Humans ; Molecular Chaperones - physiology ; Multiprotein Complexes ; Nucleolin ; Nucleosomes - metabolism ; Nucleosomes - ultrastructure ; Pathology ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - physiology ; Protein Binding ; Protein Folding ; RNA Precursors - metabolism ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - physiology ; Transcription, Genetic - physiology ; Transcriptional Elongation Factors - physiology ; Vertebrates - genetics ; Vertebrates - metabolism ; Yeasts - genetics ; Yeasts - metabolism</subject><ispartof>Trends in cell biology, 2007-02, Vol.17 (2), p.80-86</ispartof><rights>Elsevier Ltd</rights><rights>2006 Elsevier Ltd</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-f9cde1728e1090332907b73486fc0db25be2509cd68966a9c4b24dcf828502ac3</citedby><cites>FETCH-LOGICAL-c471t-f9cde1728e1090332907b73486fc0db25be2509cd68966a9c4b24dcf828502ac3</cites><orcidid>0000-0003-4524-2233</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0962892406003370$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17157503$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00337685$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Mongelard, Fabien</creatorcontrib><creatorcontrib>Bouvet, Philippe</creatorcontrib><title>Nucleolin: a multiFACeTed protein</title><title>Trends in cell biology</title><addtitle>Trends Cell Biol</addtitle><description>Nucleolin is an abundant, ubiquitously expressed protein that is found in various cell compartments, especially in the nucleolus, of which it is a major component. This multifunctional protein has been described as being a part of many pathways, from interactions with viruses at the cellular membrane to essential processing of the ribosomal RNA in the nucleolus. However, most of the molecular details of these different functions are not understood. Here, we focus on the role of nucleolin in transcription, especially some recent findings describing the protein as a histone chaperone [with functional similarity to the facilitates chromatin transcription (FACT) complex] and a chromatin co-remodeler. These new properties could help reconcile discrepancies in the literature regarding the role of nucleolin in transcription.</description><subject>Animals</subject><subject>Cell Compartmentation</subject><subject>Cell Nucleolus - metabolism</subject><subject>Cell Nucleolus - ultrastructure</subject><subject>Chromatin - chemistry</subject><subject>Chromatin - genetics</subject><subject>Chromatin - ultrastructure</subject><subject>DNA, Ribosomal - metabolism</subject><subject>DNA-Binding Proteins - physiology</subject><subject>DNA-Directed RNA Polymerases - metabolism</subject><subject>Eukaryotic Cells - metabolism</subject><subject>Eukaryotic Cells - ultrastructure</subject><subject>Fungal Proteins - physiology</subject><subject>Gene Expression Regulation</subject><subject>High Mobility Group Proteins - physiology</subject><subject>Histones - physiology</subject><subject>Humans</subject><subject>Molecular Chaperones - physiology</subject><subject>Multiprotein Complexes</subject><subject>Nucleolin</subject><subject>Nucleosomes - metabolism</subject><subject>Nucleosomes - ultrastructure</subject><subject>Pathology</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - physiology</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>RNA Precursors - metabolism</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - physiology</subject><subject>Transcription, Genetic - physiology</subject><subject>Transcriptional Elongation Factors - physiology</subject><subject>Vertebrates - genetics</subject><subject>Vertebrates - metabolism</subject><subject>Yeasts - genetics</subject><subject>Yeasts - metabolism</subject><issn>0962-8924</issn><issn>1879-3088</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2L1EAQhhtR3NnVH-BFxovgIbGqO-kPF4RhcF1h0IPruUg6Fewxk6zpZGH_vZ2dQcGDnhqKp94unleIFwg5Auq3-3zydS4BdI6YA8IjsUJrXKbA2sdiBU7LzDpZnInzGPcAYCSqp-IMDZamBLUSrz7PvuOhC_27dbU-zN0UrjZbvuFmfTsOE4f-mXjSVl3k56f3Qny7-nCzvc52Xz5-2m52mS8MTlnrfMNopGUEB0pJB6Y2qrC69dDUsqxZlpAgbZ3WlfNFLYvGt1baEmTl1YV4c8z9XnV0O4ZDNd7TUAW63uxomUFKNdqWd5jY10c23fhz5jjRIUTPXVf1PMyR0h_Wlkr_F0RnC51CE4hH0I9DjCO3v09AoEU27SnJpkU2IVKSnXZensLn-sDNn42T3QRcHgFO3u4CjxR94N5zE0b2EzVD-Gf8-7-2faop-Kr7wfcc98M89qkQQoqSgL4ubS9lg34wBeoXnGSgMg</recordid><startdate>20070201</startdate><enddate>20070201</enddate><creator>Mongelard, Fabien</creator><creator>Bouvet, Philippe</creator><general>Elsevier Ltd</general><general>Elsevier</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>7TM</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-4524-2233</orcidid></search><sort><creationdate>20070201</creationdate><title>Nucleolin: a multiFACeTed protein</title><author>Mongelard, Fabien ; Bouvet, Philippe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-f9cde1728e1090332907b73486fc0db25be2509cd68966a9c4b24dcf828502ac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Cell Compartmentation</topic><topic>Cell Nucleolus - metabolism</topic><topic>Cell Nucleolus - ultrastructure</topic><topic>Chromatin - chemistry</topic><topic>Chromatin - genetics</topic><topic>Chromatin - ultrastructure</topic><topic>DNA, Ribosomal - metabolism</topic><topic>DNA-Binding Proteins - physiology</topic><topic>DNA-Directed RNA Polymerases - metabolism</topic><topic>Eukaryotic Cells - metabolism</topic><topic>Eukaryotic Cells - ultrastructure</topic><topic>Fungal Proteins - physiology</topic><topic>Gene Expression Regulation</topic><topic>High Mobility Group Proteins - physiology</topic><topic>Histones - physiology</topic><topic>Humans</topic><topic>Molecular Chaperones - physiology</topic><topic>Multiprotein Complexes</topic><topic>Nucleolin</topic><topic>Nucleosomes - metabolism</topic><topic>Nucleosomes - ultrastructure</topic><topic>Pathology</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - physiology</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>RNA Precursors - metabolism</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - physiology</topic><topic>Transcription, Genetic - physiology</topic><topic>Transcriptional Elongation Factors - physiology</topic><topic>Vertebrates - genetics</topic><topic>Vertebrates - metabolism</topic><topic>Yeasts - genetics</topic><topic>Yeasts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mongelard, Fabien</creatorcontrib><creatorcontrib>Bouvet, Philippe</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Trends in cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mongelard, Fabien</au><au>Bouvet, Philippe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleolin: a multiFACeTed protein</atitle><jtitle>Trends in cell biology</jtitle><addtitle>Trends Cell Biol</addtitle><date>2007-02-01</date><risdate>2007</risdate><volume>17</volume><issue>2</issue><spage>80</spage><epage>86</epage><pages>80-86</pages><issn>0962-8924</issn><eissn>1879-3088</eissn><abstract>Nucleolin is an abundant, ubiquitously expressed protein that is found in various cell compartments, especially in the nucleolus, of which it is a major component. This multifunctional protein has been described as being a part of many pathways, from interactions with viruses at the cellular membrane to essential processing of the ribosomal RNA in the nucleolus. However, most of the molecular details of these different functions are not understood. Here, we focus on the role of nucleolin in transcription, especially some recent findings describing the protein as a histone chaperone [with functional similarity to the facilitates chromatin transcription (FACT) complex] and a chromatin co-remodeler. These new properties could help reconcile discrepancies in the literature regarding the role of nucleolin in transcription.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>17157503</pmid><doi>10.1016/j.tcb.2006.11.010</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-4524-2233</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0962-8924 |
ispartof | Trends in cell biology, 2007-02, Vol.17 (2), p.80-86 |
issn | 0962-8924 1879-3088 |
language | eng |
recordid | cdi_hal_primary_oai_HAL_hal_00337685v1 |
source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Animals Cell Compartmentation Cell Nucleolus - metabolism Cell Nucleolus - ultrastructure Chromatin - chemistry Chromatin - genetics Chromatin - ultrastructure DNA, Ribosomal - metabolism DNA-Binding Proteins - physiology DNA-Directed RNA Polymerases - metabolism Eukaryotic Cells - metabolism Eukaryotic Cells - ultrastructure Fungal Proteins - physiology Gene Expression Regulation High Mobility Group Proteins - physiology Histones - physiology Humans Molecular Chaperones - physiology Multiprotein Complexes Nucleolin Nucleosomes - metabolism Nucleosomes - ultrastructure Pathology Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - physiology Protein Binding Protein Folding RNA Precursors - metabolism RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - physiology Transcription, Genetic - physiology Transcriptional Elongation Factors - physiology Vertebrates - genetics Vertebrates - metabolism Yeasts - genetics Yeasts - metabolism |
title | Nucleolin: a multiFACeTed protein |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T10%3A34%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Nucleolin:%20a%20multiFACeTed%20protein&rft.jtitle=Trends%20in%20cell%20biology&rft.au=Mongelard,%20Fabien&rft.date=2007-02-01&rft.volume=17&rft.issue=2&rft.spage=80&rft.epage=86&rft.pages=80-86&rft.issn=0962-8924&rft.eissn=1879-3088&rft_id=info:doi/10.1016/j.tcb.2006.11.010&rft_dat=%3Cproquest_hal_p%3E68988536%3C/proquest_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19846768&rft_id=info:pmid/17157503&rft_els_id=S0962892406003370&rfr_iscdi=true |