Regulation of cellular actin architecture by S100A10
Actin structures are involved in several biological processes and the disruption of actin polymerisation induces impaired motility of eukaryotic cells. Different factors are involved in regulation and maintenance of the cytoskeletal actin architecture. Here we show that S100A10 participates in the p...
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| Veröffentlicht in: | Experimental cell research 2010-04, Vol.316 (7), p.1234-1240 |
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| creator | Jung, M. Juliane Murzik, Ulrike Wehder, Liane Hemmerich, Peter Melle, Christian |
| description | Actin structures are involved in several biological processes and the disruption of actin polymerisation induces impaired motility of eukaryotic cells. Different factors are involved in regulation and maintenance of the cytoskeletal actin architecture. Here we show that S100A10 participates in the particular organisation of actin filaments. Down-regulation of S100A10 by specific siRNA triggered a disorganisation of filamentous actin structures without a reduction of the total cellular actin concentration. In contrast, the formation of cytoskeleton structures containing tubulin was unhindered in S100A10 depleted cells. Interestingly, the cellular distribution of annexin A2, an interaction partner of S100A10, was unaffected in S100A10 depleted cells. Cells lacking S100A10 showed an impaired migration activity and were unable to close a scratched wound. Our data provide first insights of S100A10 function as a regulator of the filamentous actin network. |
| doi_str_mv | 10.1016/j.yexcr.2010.01.022 |
| format | Article |
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Juliane ; Murzik, Ulrike ; Wehder, Liane ; Hemmerich, Peter ; Melle, Christian</creator><creatorcontrib>Jung, M. Juliane ; Murzik, Ulrike ; Wehder, Liane ; Hemmerich, Peter ; Melle, Christian</creatorcontrib><description>Actin structures are involved in several biological processes and the disruption of actin polymerisation induces impaired motility of eukaryotic cells. Different factors are involved in regulation and maintenance of the cytoskeletal actin architecture. Here we show that S100A10 participates in the particular organisation of actin filaments. Down-regulation of S100A10 by specific siRNA triggered a disorganisation of filamentous actin structures without a reduction of the total cellular actin concentration. In contrast, the formation of cytoskeleton structures containing tubulin was unhindered in S100A10 depleted cells. Interestingly, the cellular distribution of annexin A2, an interaction partner of S100A10, was unaffected in S100A10 depleted cells. Cells lacking S100A10 showed an impaired migration activity and were unable to close a scratched wound. 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All rights reserved.</rights><rights>Copyright © 2010 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-31a5b6047847fa9ce5fc1abf3aa717c8b4ffa7f0afb980c25b4f996c21a2b7c3</citedby><cites>FETCH-LOGICAL-c451t-31a5b6047847fa9ce5fc1abf3aa717c8b4ffa7f0afb980c25b4f996c21a2b7c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.yexcr.2010.01.022$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20100475$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jung, M. Juliane</creatorcontrib><creatorcontrib>Murzik, Ulrike</creatorcontrib><creatorcontrib>Wehder, Liane</creatorcontrib><creatorcontrib>Hemmerich, Peter</creatorcontrib><creatorcontrib>Melle, Christian</creatorcontrib><title>Regulation of cellular actin architecture by S100A10</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>Actin structures are involved in several biological processes and the disruption of actin polymerisation induces impaired motility of eukaryotic cells. Different factors are involved in regulation and maintenance of the cytoskeletal actin architecture. Here we show that S100A10 participates in the particular organisation of actin filaments. Down-regulation of S100A10 by specific siRNA triggered a disorganisation of filamentous actin structures without a reduction of the total cellular actin concentration. In contrast, the formation of cytoskeleton structures containing tubulin was unhindered in S100A10 depleted cells. Interestingly, the cellular distribution of annexin A2, an interaction partner of S100A10, was unaffected in S100A10 depleted cells. Cells lacking S100A10 showed an impaired migration activity and were unable to close a scratched wound. Our data provide first insights of S100A10 function as a regulator of the filamentous actin network.</description><subject>Actin</subject><subject>Actin Cytoskeleton - chemistry</subject><subject>Actin Cytoskeleton - drug effects</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Actins - chemistry</subject><subject>Actins - metabolism</subject><subject>Annexin A2</subject><subject>Annexin A2 - antagonists & inhibitors</subject><subject>Annexin A2 - genetics</subject><subject>Annexin A2 - metabolism</subject><subject>Annexin A2 - physiology</subject><subject>Cell Movement - drug effects</subject><subject>Cell Movement - genetics</subject><subject>Cells - metabolism</subject><subject>Cells - ultrastructure</subject><subject>Cellular biology</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton - chemistry</subject><subject>Cytoskeleton - drug effects</subject><subject>Cytoskeleton - metabolism</subject><subject>Cytoskeleton architecture</subject><subject>Down-Regulation - drug effects</subject><subject>Humans</subject><subject>Migration</subject><subject>Polymerization</subject><subject>Proteins</subject><subject>RNA, Small Interfering - pharmacology</subject><subject>S100 Proteins - antagonists & inhibitors</subject><subject>S100 Proteins - genetics</subject><subject>S100 Proteins - physiology</subject><subject>S100A10</subject><subject>Tissue Distribution</subject><subject>Tubulin</subject><subject>Tumor Cells, Cultured</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1PwzAMhiMEYmPwC5BQxYVTi52mTXvgME18SZOQYPcozRJItbUjaRH796RscODAybL1vLb1EHKOkCBgfl0nW_2pXEIhTAAToPSAjBFKiCmj9JCMAZDFrKB8RE68rwGgKDA_JqMhAoxnY8Ke9Wu_kp1tm6g1kdKrVWhdJFVnm0g69WY7rbre6ajaRi8hNkU4JUdGrrw-29cJWdzdLmYP8fzp_nE2nceKZdjFKcqsysOdgnEjS6Uzo1BWJpWSI1dFxYyR3IA0VVmAolkYlGWuKEpacZVOyNVu7ca17732nVhbP3woG932XvA0LTLGGAby8g9Zt71rwm-iyGgOHBgEKN1ByrXeO23Extm1dFuBIAajohbfRsWgRwCKYDSkLvar-2qtl7-ZH4UBuNkBOpj4sNoJr6xulF5aF8yJZWv_PfAF2s2GPA</recordid><startdate>20100415</startdate><enddate>20100415</enddate><creator>Jung, M. 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Juliane</au><au>Murzik, Ulrike</au><au>Wehder, Liane</au><au>Hemmerich, Peter</au><au>Melle, Christian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of cellular actin architecture by S100A10</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>2010-04-15</date><risdate>2010</risdate><volume>316</volume><issue>7</issue><spage>1234</spage><epage>1240</epage><pages>1234-1240</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><abstract>Actin structures are involved in several biological processes and the disruption of actin polymerisation induces impaired motility of eukaryotic cells. Different factors are involved in regulation and maintenance of the cytoskeletal actin architecture. Here we show that S100A10 participates in the particular organisation of actin filaments. 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| subjects | Actin Actin Cytoskeleton - chemistry Actin Cytoskeleton - drug effects Actin Cytoskeleton - metabolism Actins - chemistry Actins - metabolism Annexin A2 Annexin A2 - antagonists & inhibitors Annexin A2 - genetics Annexin A2 - metabolism Annexin A2 - physiology Cell Movement - drug effects Cell Movement - genetics Cells - metabolism Cells - ultrastructure Cellular biology Cytoskeleton Cytoskeleton - chemistry Cytoskeleton - drug effects Cytoskeleton - metabolism Cytoskeleton architecture Down-Regulation - drug effects Humans Migration Polymerization Proteins RNA, Small Interfering - pharmacology S100 Proteins - antagonists & inhibitors S100 Proteins - genetics S100 Proteins - physiology S100A10 Tissue Distribution Tubulin Tumor Cells, Cultured |
| title | Regulation of cellular actin architecture by S100A10 |
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