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Lasp-1 Regulates Podosome Function

Please always quote using this URN: urn:nbn:de:bvb:20-opus-134315
  • Eukaryotic cells form a variety of adhesive structures to connect with their environment and to regulate cell motility. In contrast to classical focal adhesions, podosomes, highly dynamic structures of different cell types, are actively engaged in matrix remodelling and degradation. Podosomes are composed of an actin-rich core region surrounded by a ring-like structure containing signalling molecules, motor proteins as well as cytoskeleton-associated proteins. Lasp-1 is a ubiquitously expressed, actin-binding protein that is known to regulateEukaryotic cells form a variety of adhesive structures to connect with their environment and to regulate cell motility. In contrast to classical focal adhesions, podosomes, highly dynamic structures of different cell types, are actively engaged in matrix remodelling and degradation. Podosomes are composed of an actin-rich core region surrounded by a ring-like structure containing signalling molecules, motor proteins as well as cytoskeleton-associated proteins. Lasp-1 is a ubiquitously expressed, actin-binding protein that is known to regulate cytoskeleton architecture and cell migration. This multidomain protein is predominantely present at focal adhesions, however, a second pool of Lasp-1 molecules is also found at lamellipodia and vesicle-like microdomains in the cytosol. In this report, we show that Lasp-1 is a novel component and regulator of podosomes. Immunofluorescence studies reveal a localization of Lasp-1 in the podosome ring structure, where it colocalizes with zyxin and vinculin. Life cell imaging experiments demonstrate that Lasp-1 is recruited in early steps of podosome assembly. A siRNA-mediated Lasp-1 knockdown in human macrophages affects podosome dynamics as well as their matrix degradation capacity. In summary, our data indicate that Lasp-1 is a novel component of podosomes and is involved in the regulation of podosomal function.show moreshow less

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Metadaten
Author: Miriam Stölting, Christiane Wiesner, Vanessa van Vliet, Elke Butt, Hermann Pavenstädt, Stefan Linder, Joachim Kremerskothen
URN:urn:nbn:de:bvb:20-opus-134315
Document Type:Journal article
Faculties:Medizinische Fakultät / Institut für Klinische Biochemie und Pathobiochemie
Language:English
Parent Title (English):PLoS One
Year of Completion:2012
Volume:7
Issue:4
Pagenumber:e35340
Source:PLoS ONE 7(4): e35340. doi:10.1371/ journal.pone.0035340
DOI:https://doi.org/10.1371/journal.pone.0035340
Dewey Decimal Classification:6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit
Tag:actin cytoskeleton; camp signaling pathway; cancer cells; dependent protein-kinase; discrete; endothelial cells; epithelial cells; invadopodia; microdomains; phosphorylation; smooth muscle cells
Release Date:2017/07/13
Licence (German):License LogoCC BY: Creative-Commons-Lizenz: Namensnennung