Regulation of cellular actin architecture by S100A10
| Autor: | Peter Hemmerich, Christian Melle, Ulrike Murzik, Liane Wehder, M. Juliane Jung |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
biology
Cells S100 Proteins Arp2/3 complex Actin remodeling Down-Regulation macromolecular substances Cell Biology Filamentous actin Actins Cell biology Actin remodeling of neurons Actin Cytoskeleton Profilin Cell Movement biology.protein Tumor Cells Cultured Humans Tissue Distribution Actin-binding protein MDia1 RNA Small Interfering Cytoskeleton Annexin A2 |
| Zdroj: | Experimental cell research. 316(7) |
| ISSN: | 1090-2422 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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