The Arp2/3 complex: a multifunctional actin organizer
The actin-related proteins (Arps) constitute a recently characterized family of proteins, many of which function as members of multiprotein complexes. The discovery that two family members, Arp2 and Arp3, act as multifunctional organizers of actin filaments in all eukaryotes has generated much excit...
Gespeichert in:
Veröffentlicht in: | Current opinion in cell biology 1999-02, Vol.11 (1), p.117-121 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 121 |
---|---|
container_issue | 1 |
container_start_page | 117 |
container_title | Current opinion in cell biology |
container_volume | 11 |
creator | Machesky, Laura M Gould, Kathleen L |
description | The actin-related proteins (Arps) constitute a recently characterized family of proteins, many of which function as members of multiprotein complexes. The discovery that two family members, Arp2 and Arp3, act as multifunctional organizers of actin filaments in all eukaryotes has generated much excitement. Over the past two years, newly discovered properties of the Arp2/3 complex have suggested a central role in the control of actin polymerization. First, it promotes actin assembly on the surface of the motile intracellular pathogen
Listeria monocytogenes. Second, it can nucleate and cross-link actin filaments
in vitro. Third, it localizes with dynamic actin-rich spots of mammalian cells suggesting a role in protrusion; it is found in cortical actin patches in the budding and fission yeasts where it may control patch movement and cortical actin function. Clearly, the complex has a central role in actin cytoskeletal function and will be the subject of much research in the coming years. |
doi_str_mv | 10.1016/S0955-0674(99)80014-3 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69597327</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0955067499800143</els_id><sourcerecordid>69597327</sourcerecordid><originalsourceid>FETCH-LOGICAL-c427t-4076a6702d70517ca8a2966756fcf8ab3c06a2c7907bcb94cbfede23c8d187e23</originalsourceid><addsrcrecordid>eNqFkMtOwzAQRS0EouXxCaCsECxCx0lsx2xQVfGSKrGgrC3HmYBRXtgJAr6etKkQO1YzizNzdQ8hJxQuKVA-ewLJWAhcJOdSXqQANAnjHTKlqZAhJBR2yfQXmZAD798AgEMk98mEAiSCUTklbPWKwdy10SwOTFO1JX5eBTqo-rKzRV-bzja1LgM9LHXQuBdd2290R2Sv0KXH4-08JM-3N6vFfbh8vHtYzJehSSLRhQkIrrmAKBfAqDA61ZHkXDBemCLVWWyA68gICSIzmUxMVmCOUWzSfKgxLIfkbPzbuua9R9-pynqDZalrbHqvuGRSxJEYQDaCxjXeOyxU62yl3ZeioNa-1MaXWstQUqqNLxUPd6fbgD6rMP9zNQoagOsRwKHmh0WnvLFYG8ytQ9OpvLH_RPwA6bN5Dw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69597327</pqid></control><display><type>article</type><title>The Arp2/3 complex: a multifunctional actin organizer</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Machesky, Laura M ; Gould, Kathleen L</creator><creatorcontrib>Machesky, Laura M ; Gould, Kathleen L</creatorcontrib><description>The actin-related proteins (Arps) constitute a recently characterized family of proteins, many of which function as members of multiprotein complexes. The discovery that two family members, Arp2 and Arp3, act as multifunctional organizers of actin filaments in all eukaryotes has generated much excitement. Over the past two years, newly discovered properties of the Arp2/3 complex have suggested a central role in the control of actin polymerization. First, it promotes actin assembly on the surface of the motile intracellular pathogen
Listeria monocytogenes. Second, it can nucleate and cross-link actin filaments
in vitro. Third, it localizes with dynamic actin-rich spots of mammalian cells suggesting a role in protrusion; it is found in cortical actin patches in the budding and fission yeasts where it may control patch movement and cortical actin function. Clearly, the complex has a central role in actin cytoskeletal function and will be the subject of much research in the coming years.</description><identifier>ISSN: 0955-0674</identifier><identifier>EISSN: 1879-0410</identifier><identifier>DOI: 10.1016/S0955-0674(99)80014-3</identifier><identifier>PMID: 10047519</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Actin-Related Protein 2 ; Actin-Related Protein 3 ; Actins - metabolism ; Cytoskeletal Proteins ; Humans ; In Vitro Techniques ; Models, Biological ; Proteins - metabolism ; Wiskott-Aldrich Syndrome Protein ; Yeasts - metabolism</subject><ispartof>Current opinion in cell biology, 1999-02, Vol.11 (1), p.117-121</ispartof><rights>1999 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-4076a6702d70517ca8a2966756fcf8ab3c06a2c7907bcb94cbfede23c8d187e23</citedby><cites>FETCH-LOGICAL-c427t-4076a6702d70517ca8a2966756fcf8ab3c06a2c7907bcb94cbfede23c8d187e23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0955067499800143$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10047519$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Machesky, Laura M</creatorcontrib><creatorcontrib>Gould, Kathleen L</creatorcontrib><title>The Arp2/3 complex: a multifunctional actin organizer</title><title>Current opinion in cell biology</title><addtitle>Curr Opin Cell Biol</addtitle><description>The actin-related proteins (Arps) constitute a recently characterized family of proteins, many of which function as members of multiprotein complexes. The discovery that two family members, Arp2 and Arp3, act as multifunctional organizers of actin filaments in all eukaryotes has generated much excitement. Over the past two years, newly discovered properties of the Arp2/3 complex have suggested a central role in the control of actin polymerization. First, it promotes actin assembly on the surface of the motile intracellular pathogen
Listeria monocytogenes. Second, it can nucleate and cross-link actin filaments
in vitro. Third, it localizes with dynamic actin-rich spots of mammalian cells suggesting a role in protrusion; it is found in cortical actin patches in the budding and fission yeasts where it may control patch movement and cortical actin function. Clearly, the complex has a central role in actin cytoskeletal function and will be the subject of much research in the coming years.</description><subject>Actin-Related Protein 2</subject><subject>Actin-Related Protein 3</subject><subject>Actins - metabolism</subject><subject>Cytoskeletal Proteins</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Models, Biological</subject><subject>Proteins - metabolism</subject><subject>Wiskott-Aldrich Syndrome Protein</subject><subject>Yeasts - metabolism</subject><issn>0955-0674</issn><issn>1879-0410</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EouXxCaCsECxCx0lsx2xQVfGSKrGgrC3HmYBRXtgJAr6etKkQO1YzizNzdQ8hJxQuKVA-ewLJWAhcJOdSXqQANAnjHTKlqZAhJBR2yfQXmZAD798AgEMk98mEAiSCUTklbPWKwdy10SwOTFO1JX5eBTqo-rKzRV-bzja1LgM9LHXQuBdd2290R2Sv0KXH4-08JM-3N6vFfbh8vHtYzJehSSLRhQkIrrmAKBfAqDA61ZHkXDBemCLVWWyA68gICSIzmUxMVmCOUWzSfKgxLIfkbPzbuua9R9-pynqDZalrbHqvuGRSxJEYQDaCxjXeOyxU62yl3ZeioNa-1MaXWstQUqqNLxUPd6fbgD6rMP9zNQoagOsRwKHmh0WnvLFYG8ytQ9OpvLH_RPwA6bN5Dw</recordid><startdate>19990201</startdate><enddate>19990201</enddate><creator>Machesky, Laura M</creator><creator>Gould, Kathleen L</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>19990201</creationdate><title>The Arp2/3 complex: a multifunctional actin organizer</title><author>Machesky, Laura M ; Gould, Kathleen L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-4076a6702d70517ca8a2966756fcf8ab3c06a2c7907bcb94cbfede23c8d187e23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Actin-Related Protein 2</topic><topic>Actin-Related Protein 3</topic><topic>Actins - metabolism</topic><topic>Cytoskeletal Proteins</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Models, Biological</topic><topic>Proteins - metabolism</topic><topic>Wiskott-Aldrich Syndrome Protein</topic><topic>Yeasts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Machesky, Laura M</creatorcontrib><creatorcontrib>Gould, Kathleen L</creatorcontrib><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><jtitle>Current opinion in cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Machesky, Laura M</au><au>Gould, Kathleen L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Arp2/3 complex: a multifunctional actin organizer</atitle><jtitle>Current opinion in cell biology</jtitle><addtitle>Curr Opin Cell Biol</addtitle><date>1999-02-01</date><risdate>1999</risdate><volume>11</volume><issue>1</issue><spage>117</spage><epage>121</epage><pages>117-121</pages><issn>0955-0674</issn><eissn>1879-0410</eissn><abstract>The actin-related proteins (Arps) constitute a recently characterized family of proteins, many of which function as members of multiprotein complexes. The discovery that two family members, Arp2 and Arp3, act as multifunctional organizers of actin filaments in all eukaryotes has generated much excitement. Over the past two years, newly discovered properties of the Arp2/3 complex have suggested a central role in the control of actin polymerization. First, it promotes actin assembly on the surface of the motile intracellular pathogen
Listeria monocytogenes. Second, it can nucleate and cross-link actin filaments
in vitro. Third, it localizes with dynamic actin-rich spots of mammalian cells suggesting a role in protrusion; it is found in cortical actin patches in the budding and fission yeasts where it may control patch movement and cortical actin function. Clearly, the complex has a central role in actin cytoskeletal function and will be the subject of much research in the coming years.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>10047519</pmid><doi>10.1016/S0955-0674(99)80014-3</doi><tpages>5</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0955-0674 |
ispartof | Current opinion in cell biology, 1999-02, Vol.11 (1), p.117-121 |
issn | 0955-0674 1879-0410 |
language | eng |
recordid | cdi_proquest_miscellaneous_69597327 |
source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Actin-Related Protein 2 Actin-Related Protein 3 Actins - metabolism Cytoskeletal Proteins Humans In Vitro Techniques Models, Biological Proteins - metabolism Wiskott-Aldrich Syndrome Protein Yeasts - metabolism |
title | The Arp2/3 complex: a multifunctional actin organizer |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T08%3A24%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Arp2/3%20complex:%20a%20multifunctional%20actin%20organizer&rft.jtitle=Current%20opinion%20in%20cell%20biology&rft.au=Machesky,%20Laura%20M&rft.date=1999-02-01&rft.volume=11&rft.issue=1&rft.spage=117&rft.epage=121&rft.pages=117-121&rft.issn=0955-0674&rft.eissn=1879-0410&rft_id=info:doi/10.1016/S0955-0674(99)80014-3&rft_dat=%3Cproquest_cross%3E69597327%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=69597327&rft_id=info:pmid/10047519&rft_els_id=S0955067499800143&rfr_iscdi=true |