How depolymerization can promote polymerization: the case of actin and profilin
Rapid polymerization and depolymerization of actin filaments in response to extracellular stimuli is required for normal cell motility and development. Profilin is one of the most important actin-binding proteins; it regulates actin polymerization and interacts with many cytoskeletal proteins that l...
Gespeichert in:
| Veröffentlicht in: | BioEssays 2009-11, Vol.31 (11), p.1150-1160 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1160 |
|---|---|
| container_issue | 11 |
| container_start_page | 1150 |
| container_title | BioEssays |
| container_volume | 31 |
| creator | Yarmola, Elena G Bubb, Michael R |
| description | Rapid polymerization and depolymerization of actin filaments in response to extracellular stimuli is required for normal cell motility and development. Profilin is one of the most important actin-binding proteins; it regulates actin polymerization and interacts with many cytoskeletal proteins that link actin to extracellular membrane. The molecular mechanism of profilin has been extensively considered and debated in the literature for over two decades. Here we discuss several accepted hypotheses regarding the mechanism of profilin function as well as new recently emerged possibilities. Thermal noise is routine in molecular world and unsurprisingly, nature has found a way to utilize it. An increasing amount of theoretical and experimental research suggests that fluctuation-based processes play important roles in many cell events. Here we show how a fluctuation-based process of exchange diffusion is involved in the regulation of actin polymerization. |
| doi_str_mv | 10.1002/bies.200900049 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_734102830</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>734102830</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4729-bd54fe1a021a66bbf58ba308981c7e786684acbc1eac97873cc7e901915124883</originalsourceid><addsrcrecordid>eNqFkEFv1DAQRi0EotvClSPkxinLjO3ENjeoSluxokJQerQc7wQMSbzEWbXLr8errAqcOI00875vpMfYM4QlAvBXTaC05AAGAKR5wBZYcSxRK_2QLYDXVWm4VEfsOKXvGTE1l4_ZERplKglqwa4u4m2xpk3sdj2N4ZebQhwK74ZiM8Y-TlT8e3pdTN8o3xMVsS2cn8JQuGG9p9vQheEJe9S6LtHTwzxh1-_OPp9elKur88vTN6vSS8VN2awr2RI64OjqumnaSjdOgDYavSKl61pL5xuP5LxRWgmf1wbQYIVcai1O2Mu5Nz_-uaU02T4kT13nBorbZJWQCFwLyORyJv0YUxqptZsx9G7cWQS7d2j3Du29wxx4fqjeNj2t_-AHaRkwM3AbOtr9p86-vTz79Hd5OWdDmujuPuvGH7ZWQlX25sO55fLLSr6_-WhF5l_MfOuidV_HkOx1rkMBqACyDPEbujKWPg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>734102830</pqid></control><display><type>article</type><title>How depolymerization can promote polymerization: the case of actin and profilin</title><source>Wiley-Blackwell Journals</source><source>MEDLINE</source><creator>Yarmola, Elena G ; Bubb, Michael R</creator><creatorcontrib>Yarmola, Elena G ; Bubb, Michael R</creatorcontrib><description>Rapid polymerization and depolymerization of actin filaments in response to extracellular stimuli is required for normal cell motility and development. Profilin is one of the most important actin-binding proteins; it regulates actin polymerization and interacts with many cytoskeletal proteins that link actin to extracellular membrane. The molecular mechanism of profilin has been extensively considered and debated in the literature for over two decades. Here we discuss several accepted hypotheses regarding the mechanism of profilin function as well as new recently emerged possibilities. Thermal noise is routine in molecular world and unsurprisingly, nature has found a way to utilize it. An increasing amount of theoretical and experimental research suggests that fluctuation-based processes play important roles in many cell events. Here we show how a fluctuation-based process of exchange diffusion is involved in the regulation of actin polymerization.</description><identifier>ISSN: 0265-9247</identifier><identifier>EISSN: 1521-1878</identifier><identifier>DOI: 10.1002/bies.200900049</identifier><identifier>PMID: 19795407</identifier><language>eng</language><publisher>Weinheim: Wiley-VCH Verlag</publisher><subject>actin ; Actins - chemistry ; Actins - physiology ; Adenosine Diphosphate - chemistry ; Adenosine Triphosphate - chemistry ; Animals ; ATP hydrolysis ; Biochemistry - methods ; Cytoskeleton - metabolism ; Diffusion ; exchange diffusion ; fluctuations ; Hot Temperature ; Humans ; Hydrolysis ; Kinetics ; Models, Biological ; profilin ; Profilins - chemistry ; Profilins - physiology ; Stochastic Processes ; Thermodynamics</subject><ispartof>BioEssays, 2009-11, Vol.31 (11), p.1150-1160</ispartof><rights>Copyright © 2009 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4729-bd54fe1a021a66bbf58ba308981c7e786684acbc1eac97873cc7e901915124883</citedby><cites>FETCH-LOGICAL-c4729-bd54fe1a021a66bbf58ba308981c7e786684acbc1eac97873cc7e901915124883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbies.200900049$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbies.200900049$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19795407$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yarmola, Elena G</creatorcontrib><creatorcontrib>Bubb, Michael R</creatorcontrib><title>How depolymerization can promote polymerization: the case of actin and profilin</title><title>BioEssays</title><addtitle>Bioessays</addtitle><description>Rapid polymerization and depolymerization of actin filaments in response to extracellular stimuli is required for normal cell motility and development. Profilin is one of the most important actin-binding proteins; it regulates actin polymerization and interacts with many cytoskeletal proteins that link actin to extracellular membrane. The molecular mechanism of profilin has been extensively considered and debated in the literature for over two decades. Here we discuss several accepted hypotheses regarding the mechanism of profilin function as well as new recently emerged possibilities. Thermal noise is routine in molecular world and unsurprisingly, nature has found a way to utilize it. An increasing amount of theoretical and experimental research suggests that fluctuation-based processes play important roles in many cell events. Here we show how a fluctuation-based process of exchange diffusion is involved in the regulation of actin polymerization.</description><subject>actin</subject><subject>Actins - chemistry</subject><subject>Actins - physiology</subject><subject>Adenosine Diphosphate - chemistry</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>Animals</subject><subject>ATP hydrolysis</subject><subject>Biochemistry - methods</subject><subject>Cytoskeleton - metabolism</subject><subject>Diffusion</subject><subject>exchange diffusion</subject><subject>fluctuations</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Models, Biological</subject><subject>profilin</subject><subject>Profilins - chemistry</subject><subject>Profilins - physiology</subject><subject>Stochastic Processes</subject><subject>Thermodynamics</subject><issn>0265-9247</issn><issn>1521-1878</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEFv1DAQRi0EotvClSPkxinLjO3ENjeoSluxokJQerQc7wQMSbzEWbXLr8errAqcOI00875vpMfYM4QlAvBXTaC05AAGAKR5wBZYcSxRK_2QLYDXVWm4VEfsOKXvGTE1l4_ZERplKglqwa4u4m2xpk3sdj2N4ZebQhwK74ZiM8Y-TlT8e3pdTN8o3xMVsS2cn8JQuGG9p9vQheEJe9S6LtHTwzxh1-_OPp9elKur88vTN6vSS8VN2awr2RI64OjqumnaSjdOgDYavSKl61pL5xuP5LxRWgmf1wbQYIVcai1O2Mu5Nz_-uaU02T4kT13nBorbZJWQCFwLyORyJv0YUxqptZsx9G7cWQS7d2j3Du29wxx4fqjeNj2t_-AHaRkwM3AbOtr9p86-vTz79Hd5OWdDmujuPuvGH7ZWQlX25sO55fLLSr6_-WhF5l_MfOuidV_HkOx1rkMBqACyDPEbujKWPg</recordid><startdate>200911</startdate><enddate>200911</enddate><creator>Yarmola, Elena G</creator><creator>Bubb, Michael R</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>FBQ</scope><scope>BSCLL</scope><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>200911</creationdate><title>How depolymerization can promote polymerization: the case of actin and profilin</title><author>Yarmola, Elena G ; Bubb, Michael R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4729-bd54fe1a021a66bbf58ba308981c7e786684acbc1eac97873cc7e901915124883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>actin</topic><topic>Actins - chemistry</topic><topic>Actins - physiology</topic><topic>Adenosine Diphosphate - chemistry</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>Animals</topic><topic>ATP hydrolysis</topic><topic>Biochemistry - methods</topic><topic>Cytoskeleton - metabolism</topic><topic>Diffusion</topic><topic>exchange diffusion</topic><topic>fluctuations</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Models, Biological</topic><topic>profilin</topic><topic>Profilins - chemistry</topic><topic>Profilins - physiology</topic><topic>Stochastic Processes</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yarmola, Elena G</creatorcontrib><creatorcontrib>Bubb, Michael R</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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>BioEssays</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yarmola, Elena G</au><au>Bubb, Michael R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>How depolymerization can promote polymerization: the case of actin and profilin</atitle><jtitle>BioEssays</jtitle><addtitle>Bioessays</addtitle><date>2009-11</date><risdate>2009</risdate><volume>31</volume><issue>11</issue><spage>1150</spage><epage>1160</epage><pages>1150-1160</pages><issn>0265-9247</issn><eissn>1521-1878</eissn><abstract>Rapid polymerization and depolymerization of actin filaments in response to extracellular stimuli is required for normal cell motility and development. Profilin is one of the most important actin-binding proteins; it regulates actin polymerization and interacts with many cytoskeletal proteins that link actin to extracellular membrane. The molecular mechanism of profilin has been extensively considered and debated in the literature for over two decades. Here we discuss several accepted hypotheses regarding the mechanism of profilin function as well as new recently emerged possibilities. Thermal noise is routine in molecular world and unsurprisingly, nature has found a way to utilize it. An increasing amount of theoretical and experimental research suggests that fluctuation-based processes play important roles in many cell events. Here we show how a fluctuation-based process of exchange diffusion is involved in the regulation of actin polymerization.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>19795407</pmid><doi>10.1002/bies.200900049</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0265-9247 |
| ispartof | BioEssays, 2009-11, Vol.31 (11), p.1150-1160 |
| issn | 0265-9247 1521-1878 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_734102830 |
| source | Wiley-Blackwell Journals; MEDLINE |
| subjects | actin Actins - chemistry Actins - physiology Adenosine Diphosphate - chemistry Adenosine Triphosphate - chemistry Animals ATP hydrolysis Biochemistry - methods Cytoskeleton - metabolism Diffusion exchange diffusion fluctuations Hot Temperature Humans Hydrolysis Kinetics Models, Biological profilin Profilins - chemistry Profilins - physiology Stochastic Processes Thermodynamics |
| title | How depolymerization can promote polymerization: the case of actin and profilin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T15%3A29%3A56IST&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=How%20depolymerization%20can%20promote%20polymerization:%20the%20case%20of%20actin%20and%20profilin&rft.jtitle=BioEssays&rft.au=Yarmola,%20Elena%20G&rft.date=2009-11&rft.volume=31&rft.issue=11&rft.spage=1150&rft.epage=1160&rft.pages=1150-1160&rft.issn=0265-9247&rft.eissn=1521-1878&rft_id=info:doi/10.1002/bies.200900049&rft_dat=%3Cproquest_cross%3E734102830%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=734102830&rft_id=info:pmid/19795407&rfr_iscdi=true |