TY  - JOUR
A1  - Stölting, Miriam
A1  - Wiesner, Christiane
A1  - van Vliet, Vanessa
A1  - Butt, Elke
A1  - Pavenstädt, Hermann
A1  - Linder, Stefan
A1  - Kremerskothen, Joachim
T1  - Lasp-1 Regulates Podosome Function
JF  - PLoS One
N2  - 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 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.
KW  - discrete
KW  - smooth muscle cells
KW  - microdomains
KW  - actin cytoskeleton
KW  - endothelial cells
KW  - epithelial cells
KW  - cancer cells
KW  - phosphorylation
KW  - invadopodia
KW  - dependent protein-kinase
KW  - camp signaling pathway
Y1  - 2012
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-134315
VL  - 7
IS  - 4
ER  -