Research ExplorerPublicationsLasp-1 regulates podosome function.

Lasp-1 regulates podosome function.

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Lasp-1 regulates podosome function. / Stölting, Miriam; Wiesner, Christiane; van Vliet, Vanessa; Butt, Elke; Pavenstädt, Hermann; Linder, Stefan; Kremerskothen, Joachim.

In: PLOS ONE, Vol. 7, No. 4, 4, 2012, p. 35340.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Stölting, M, Wiesner, C, van Vliet, V, Butt, E, Pavenstädt, H, Linder, S & Kremerskothen, J 2012, 'Lasp-1 regulates podosome function.', PLOS ONE, vol. 7, no. 4, 4, pp. 35340. https://doi.org/10.1371/journal.pone.0035340

APA

Stölting, M., Wiesner, C., van Vliet, V., Butt, E., Pavenstädt, H., Linder, S., & Kremerskothen, J. (2012). Lasp-1 regulates podosome function. PLOS ONE, 7(4), 35340. [4]. https://doi.org/10.1371/journal.pone.0035340

Vancouver

Stölting M, Wiesner C, van Vliet V, Butt E, Pavenstädt H, Linder S et al. Lasp-1 regulates podosome function. PLOS ONE. 2012;7(4):35340. 4. https://doi.org/10.1371/journal.pone.0035340

Bibtex

@article{d0843f3180db44b9bf694de29baac3fa,
title = "Lasp-1 regulates podosome function.",
abstract = "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.",
keywords = "Animals, Humans, Cells, Cultured, Rats, Cell Line, Nerve Tissue Proteins/genetics/*metabolism, RNA, Small Interfering/genetics, Macrophages/metabolism, Pseudopodia/*metabolism, Cytoskeletal Proteins/genetics/*metabolism, Adaptor Proteins, Signal Transducing/genetics/*metabolism, Cytoskeleton/*metabolism, Focal Adhesions/metabolism, LIM Domain Proteins/genetics/*metabolism, Microfilament Proteins/genetics/*metabolism, Vinculin/metabolism, Zyxin/metabolism, Animals, Humans, Cells, Cultured, Rats, Cell Line, Nerve Tissue Proteins/genetics/*metabolism, RNA, Small Interfering/genetics, Macrophages/metabolism, Pseudopodia/*metabolism, Cytoskeletal Proteins/genetics/*metabolism, Adaptor Proteins, Signal Transducing/genetics/*metabolism, Cytoskeleton/*metabolism, Focal Adhesions/metabolism, LIM Domain Proteins/genetics/*metabolism, Microfilament Proteins/genetics/*metabolism, Vinculin/metabolism, Zyxin/metabolism",
author = "Miriam St{\"o}lting and Christiane Wiesner and {van Vliet}, Vanessa and Elke Butt and Hermann Pavenst{\"a}dt and Stefan Linder and Joachim Kremerskothen",
year = "2012",
doi = "10.1371/journal.pone.0035340",
language = "English",
volume = "7",
pages = "35340",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "4",

}

RIS

TY - JOUR

T1 - Lasp-1 regulates podosome function.

AU - Stölting, Miriam

AU - Wiesner, Christiane

AU - van Vliet, Vanessa

AU - Butt, Elke

AU - Pavenstädt, Hermann

AU - Linder, Stefan

AU - Kremerskothen, Joachim

PY - 2012

Y1 - 2012

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.

AB - 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 - Animals

KW - Humans

KW - Cells, Cultured

KW - Rats

KW - Cell Line

KW - Nerve Tissue Proteins/genetics/metabolism

KW - RNA, Small Interfering/genetics

KW - Macrophages/metabolism

KW - Pseudopodia/metabolism

KW - Cytoskeletal Proteins/genetics/metabolism

KW - Adaptor Proteins, Signal Transducing/genetics/metabolism

KW - Cytoskeleton/metabolism

KW - Focal Adhesions/metabolism

KW - LIM Domain Proteins/genetics/metabolism

KW - Microfilament Proteins/genetics/metabolism

KW - Vinculin/metabolism

KW - Zyxin/metabolism

KW - Animals

KW - Humans

KW - Cells, Cultured

KW - Rats

KW - Cell Line

KW - Nerve Tissue Proteins/genetics/metabolism

KW - RNA, Small Interfering/genetics

KW - Macrophages/metabolism

KW - Pseudopodia/metabolism

KW - Cytoskeletal Proteins/genetics/metabolism

KW - Adaptor Proteins, Signal Transducing/genetics/metabolism

KW - Cytoskeleton/metabolism

KW - Focal Adhesions/metabolism

KW - LIM Domain Proteins/genetics/metabolism

KW - Microfilament Proteins/genetics/metabolism

KW - Vinculin/metabolism

KW - Zyxin/metabolism

U2 - 10.1371/journal.pone.0035340

DO - 10.1371/journal.pone.0035340

M3 - SCORING: Journal article

VL - 7

SP - 35340

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 4

M1 - 4

ER -