Loading…

Molecular details of formin-mediated actin assembly

Formins are a large family of multi-domain polypeptides that form homodimers. The highly conserved formin homology 2 (FH2) domain and its neighboring formin homology 1 (FH1) domain, which are surrounded by regulatory domains, cooperate in rapidly assembling profilin–actin into long filaments while r...

Full description

Saved in:

Bibliographic Details
Published in:	Current opinion in cell biology 2006-02, Vol.18 (1), p.11-17
Main Author:	Kovar, David R
Format:	Article
Language:	English
Subjects:	Actin Cytoskeleton - chemistry Actin Cytoskeleton - metabolism Actin Cytoskeleton - ultrastructure Actins - chemistry Actins - metabolism Animals Biopolymers - chemistry Carrier Proteins - chemistry Carrier Proteins - genetics Contractile Proteins - metabolism Microfilament Proteins - chemistry Microfilament Proteins - physiology Models, Biological Profilins - chemistry Protein Structure, Tertiary
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by	cdi_FETCH-LOGICAL-c465t-944726eae6bfd0fe82da166927ec16e9b02693145dac7e56382af77d30d9e87c3
cites	cdi_FETCH-LOGICAL-c465t-944726eae6bfd0fe82da166927ec16e9b02693145dac7e56382af77d30d9e87c3
container_end_page	17
container_issue	1
container_start_page	11
container_title	Current opinion in cell biology
container_volume	18
creator	Kovar, David R
description	Formins are a large family of multi-domain polypeptides that form homodimers. The highly conserved formin homology 2 (FH2) domain and its neighboring formin homology 1 (FH1) domain, which are surrounded by regulatory domains, cooperate in rapidly assembling profilin–actin into long filaments while remaining continuously associated with the fast-growing barbed end. Recent biochemical, biophysical, theoretical and structural studies have concluded that diverse formins are mechanistically similar, but that the rates of various assembly states differ quantitatively, and have shed light on the mechanism of formin auto-regulation and activation by Rho GTPases.
doi_str_mv	10.1016/j.ceb.2005.12.011
format	article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70697553</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0955067405001912</els_id><sourcerecordid>70697553</sourcerecordid><originalsourceid>FETCH-LOGICAL-c465t-944726eae6bfd0fe82da166927ec16e9b02693145dac7e56382af77d30d9e87c3</originalsourceid><addsrcrecordid>eNp9kEtLxDAUhYMozjj6A9xIV-5ab9I8GlyJ-IIRN7oOaXILGfoYk1aYf2-HGXDn6my-c-B8hFxTKChQebcpHNYFAxAFZQVQekKWtFI6B07hlCxBC5GDVHxBLlLaAIAEps_JgspScsn4kpTvQ4tuam3MPI42tCkbmqwZYhf6vEMf7Ig-s24MfWZTwq5ud5fkrLFtwqtjrsjX89Pn42u-_nh5e3xY545LMeaac8UkWpR146HBinlLpdRMoaMSdQ1M6pJy4a1TKGRZMdso5UvwGivlyhW5Pexu4_A9YRpNF5LDtrU9DlMyCqRWQpQzSA-gi0NKERuzjaGzcWcomL0pszGzKbM3ZSgzs6m5c3Mcn-r551_jqGYG7g8Azhd_AkaTXMDezU4iutH4Ifwz_wsMFXgY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>70697553</pqid></control><display><type>article</type><title>Molecular details of formin-mediated actin assembly</title><source>ScienceDirect Freedom Collection 2022-2024</source><creator>Kovar, David R</creator><creatorcontrib>Kovar, David R</creatorcontrib><description>Formins are a large family of multi-domain polypeptides that form homodimers. The highly conserved formin homology 2 (FH2) domain and its neighboring formin homology 1 (FH1) domain, which are surrounded by regulatory domains, cooperate in rapidly assembling profilin–actin into long filaments while remaining continuously associated with the fast-growing barbed end. Recent biochemical, biophysical, theoretical and structural studies have concluded that diverse formins are mechanistically similar, but that the rates of various assembly states differ quantitatively, and have shed light on the mechanism of formin auto-regulation and activation by Rho GTPases.</description><identifier>ISSN: 0955-0674</identifier><identifier>EISSN: 1879-0410</identifier><identifier>DOI: 10.1016/j.ceb.2005.12.011</identifier><identifier>PMID: 16364624</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Actin Cytoskeleton - chemistry ; Actin Cytoskeleton - metabolism ; Actin Cytoskeleton - ultrastructure ; Actins - chemistry ; Actins - metabolism ; Animals ; Biopolymers - chemistry ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Contractile Proteins - metabolism ; Microfilament Proteins - chemistry ; Microfilament Proteins - physiology ; Models, Biological ; Profilins - chemistry ; Protein Structure, Tertiary</subject><ispartof>Current opinion in cell biology, 2006-02, Vol.18 (1), p.11-17</ispartof><rights>2006 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c465t-944726eae6bfd0fe82da166927ec16e9b02693145dac7e56382af77d30d9e87c3</citedby><cites>FETCH-LOGICAL-c465t-944726eae6bfd0fe82da166927ec16e9b02693145dac7e56382af77d30d9e87c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16364624$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kovar, David R</creatorcontrib><title>Molecular details of formin-mediated actin assembly</title><title>Current opinion in cell biology</title><addtitle>Curr Opin Cell Biol</addtitle><description>Formins are a large family of multi-domain polypeptides that form homodimers. The highly conserved formin homology 2 (FH2) domain and its neighboring formin homology 1 (FH1) domain, which are surrounded by regulatory domains, cooperate in rapidly assembling profilin–actin into long filaments while remaining continuously associated with the fast-growing barbed end. Recent biochemical, biophysical, theoretical and structural studies have concluded that diverse formins are mechanistically similar, but that the rates of various assembly states differ quantitatively, and have shed light on the mechanism of formin auto-regulation and activation by Rho GTPases.</description><subject>Actin Cytoskeleton - chemistry</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Actin Cytoskeleton - ultrastructure</subject><subject>Actins - chemistry</subject><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Biopolymers - chemistry</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Contractile Proteins - metabolism</subject><subject>Microfilament Proteins - chemistry</subject><subject>Microfilament Proteins - physiology</subject><subject>Models, Biological</subject><subject>Profilins - chemistry</subject><subject>Protein Structure, Tertiary</subject><issn>0955-0674</issn><issn>1879-0410</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNp9kEtLxDAUhYMozjj6A9xIV-5ab9I8GlyJ-IIRN7oOaXILGfoYk1aYf2-HGXDn6my-c-B8hFxTKChQebcpHNYFAxAFZQVQekKWtFI6B07hlCxBC5GDVHxBLlLaAIAEps_JgspScsn4kpTvQ4tuam3MPI42tCkbmqwZYhf6vEMf7Ig-s24MfWZTwq5ud5fkrLFtwqtjrsjX89Pn42u-_nh5e3xY545LMeaac8UkWpR146HBinlLpdRMoaMSdQ1M6pJy4a1TKGRZMdso5UvwGivlyhW5Pexu4_A9YRpNF5LDtrU9DlMyCqRWQpQzSA-gi0NKERuzjaGzcWcomL0pszGzKbM3ZSgzs6m5c3Mcn-r551_jqGYG7g8Azhd_AkaTXMDezU4iutH4Ifwz_wsMFXgY</recordid><startdate>20060201</startdate><enddate>20060201</enddate><creator>Kovar, David R</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>20060201</creationdate><title>Molecular details of formin-mediated actin assembly</title><author>Kovar, David R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c465t-944726eae6bfd0fe82da166927ec16e9b02693145dac7e56382af77d30d9e87c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Actin Cytoskeleton - chemistry</topic><topic>Actin Cytoskeleton - metabolism</topic><topic>Actin Cytoskeleton - ultrastructure</topic><topic>Actins - chemistry</topic><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Biopolymers - chemistry</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Contractile Proteins - metabolism</topic><topic>Microfilament Proteins - chemistry</topic><topic>Microfilament Proteins - physiology</topic><topic>Models, Biological</topic><topic>Profilins - chemistry</topic><topic>Protein Structure, Tertiary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kovar, David R</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>Kovar, David R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular details of formin-mediated actin assembly</atitle><jtitle>Current opinion in cell biology</jtitle><addtitle>Curr Opin Cell Biol</addtitle><date>2006-02-01</date><risdate>2006</risdate><volume>18</volume><issue>1</issue><spage>11</spage><epage>17</epage><pages>11-17</pages><issn>0955-0674</issn><eissn>1879-0410</eissn><abstract>Formins are a large family of multi-domain polypeptides that form homodimers. The highly conserved formin homology 2 (FH2) domain and its neighboring formin homology 1 (FH1) domain, which are surrounded by regulatory domains, cooperate in rapidly assembling profilin–actin into long filaments while remaining continuously associated with the fast-growing barbed end. Recent biochemical, biophysical, theoretical and structural studies have concluded that diverse formins are mechanistically similar, but that the rates of various assembly states differ quantitatively, and have shed light on the mechanism of formin auto-regulation and activation by Rho GTPases.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>16364624</pmid><doi>10.1016/j.ceb.2005.12.011</doi><tpages>7</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0955-0674
ispartof	Current opinion in cell biology, 2006-02, Vol.18 (1), p.11-17
issn	0955-0674 1879-0410
language	eng
recordid	cdi_proquest_miscellaneous_70697553
source	ScienceDirect Freedom Collection 2022-2024
subjects	Actin Cytoskeleton - chemistry Actin Cytoskeleton - metabolism Actin Cytoskeleton - ultrastructure Actins - chemistry Actins - metabolism Animals Biopolymers - chemistry Carrier Proteins - chemistry Carrier Proteins - genetics Contractile Proteins - metabolism Microfilament Proteins - chemistry Microfilament Proteins - physiology Models, Biological Profilins - chemistry Protein Structure, Tertiary
title	Molecular details of formin-mediated actin assembly
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T05%3A22%3A05IST&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=Molecular%20details%20of%20formin-mediated%20actin%20assembly&rft.jtitle=Current%20opinion%20in%20cell%20biology&rft.au=Kovar,%20David%20R&rft.date=2006-02-01&rft.volume=18&rft.issue=1&rft.spage=11&rft.epage=17&rft.pages=11-17&rft.issn=0955-0674&rft.eissn=1879-0410&rft_id=info:doi/10.1016/j.ceb.2005.12.011&rft_dat=%3Cproquest_cross%3E70697553%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c465t-944726eae6bfd0fe82da166927ec16e9b02693145dac7e56382af77d30d9e87c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=70697553&rft_id=info:pmid/16364624&rfr_iscdi=true