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Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism.

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Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism. / Windhorst, Sabine; Blechner, Christine; Lin, Hongying; Elling, Christian; Nalaskowski, Marcus; Kirchberger, Tanja; Guse, Andreas H.; Mayr, Georg W.

In: BIOCHEM J, Vol. 414, No. 3, 3, 2008, p. 407-417.

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

Harvard

Windhorst, S, Blechner, C, Lin, H, Elling, C, Nalaskowski, M, Kirchberger, T, Guse, AH & Mayr, GW 2008, 'Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism.', BIOCHEM J, vol. 414, no. 3, 3, pp. 407-417. <http://www.ncbi.nlm.nih.gov/pubmed/18498254?dopt=Citation>

APA

Windhorst, S., Blechner, C., Lin, H., Elling, C., Nalaskowski, M., Kirchberger, T., Guse, A. H., & Mayr, G. W. (2008). Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism. BIOCHEM J, 414(3), 407-417. [3]. http://www.ncbi.nlm.nih.gov/pubmed/18498254?dopt=Citation

Vancouver

Windhorst S, Blechner C, Lin H, Elling C, Nalaskowski M, Kirchberger T et al. Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism. BIOCHEM J. 2008;414(3):407-417. 3.

Bibtex

@article{f6a3e32d91b64fef97c3ae1c2ac1acc1,
title = "Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism.",
abstract = "In the present study, effects of increased IP3K-A [Ins(1,4,5)P(3) 3-kinase-A] expression were analysed. H1299 cells overexpressing IP3K-A formed branching protrusions, and under three-dimensional culture conditions, they exhibited a motile fibroblast-like morphology. They lost the ability to form actin stress fibres and showed increased invasive migration in vitro. Furthermore, expression levels of the mesenchymal marker proteins vimentin and N-cadherin were increased. The enzymatic function of IP3K-A is to phosphorylate the calcium-mobilizing second messenger Ins(1,4,5)P(3) to (Ins(1,3,4,5)P(4). Accordingly, cells overexpressing IP3K-A showed reduced calcium release and altered concentrations of InsPs, with decreasing concentrations of Ins(1,4,5)P(3), InsP(6) and Ins(1,2,3,4,5)P(5), and increasing concentrations of Ins(1,3,4,5)P(4). However, IP3K-A-induced effects on cell morphology do not seem to be dependent on enzyme activity, since a protein devoid of enzyme activity also induced the formation of branching protrusions. Therefore we propose that the morphological changes induced by IP3K-A are mediated by non-enzymatic activities of the protein.",
author = "Sabine Windhorst and Christine Blechner and Hongying Lin and Christian Elling and Marcus Nalaskowski and Tanja Kirchberger and Guse, {Andreas H.} and Mayr, {Georg W.}",
year = "2008",
language = "Deutsch",
volume = "414",
pages = "407--417",
journal = "BIOCHEM J",
issn = "0264-6021",
publisher = "PORTLAND PRESS LTD",
number = "3",

}

RIS

TY - JOUR

T1 - Ins(1,4,5)P3 3-kinase-A overexpression induces cytoskeletal reorganization via a kinase-independent mechanism.

AU - Windhorst, Sabine

AU - Blechner, Christine

AU - Lin, Hongying

AU - Elling, Christian

AU - Nalaskowski, Marcus

AU - Kirchberger, Tanja

AU - Guse, Andreas H.

AU - Mayr, Georg W.

PY - 2008

Y1 - 2008

N2 - In the present study, effects of increased IP3K-A [Ins(1,4,5)P(3) 3-kinase-A] expression were analysed. H1299 cells overexpressing IP3K-A formed branching protrusions, and under three-dimensional culture conditions, they exhibited a motile fibroblast-like morphology. They lost the ability to form actin stress fibres and showed increased invasive migration in vitro. Furthermore, expression levels of the mesenchymal marker proteins vimentin and N-cadherin were increased. The enzymatic function of IP3K-A is to phosphorylate the calcium-mobilizing second messenger Ins(1,4,5)P(3) to (Ins(1,3,4,5)P(4). Accordingly, cells overexpressing IP3K-A showed reduced calcium release and altered concentrations of InsPs, with decreasing concentrations of Ins(1,4,5)P(3), InsP(6) and Ins(1,2,3,4,5)P(5), and increasing concentrations of Ins(1,3,4,5)P(4). However, IP3K-A-induced effects on cell morphology do not seem to be dependent on enzyme activity, since a protein devoid of enzyme activity also induced the formation of branching protrusions. Therefore we propose that the morphological changes induced by IP3K-A are mediated by non-enzymatic activities of the protein.

AB - In the present study, effects of increased IP3K-A [Ins(1,4,5)P(3) 3-kinase-A] expression were analysed. H1299 cells overexpressing IP3K-A formed branching protrusions, and under three-dimensional culture conditions, they exhibited a motile fibroblast-like morphology. They lost the ability to form actin stress fibres and showed increased invasive migration in vitro. Furthermore, expression levels of the mesenchymal marker proteins vimentin and N-cadherin were increased. The enzymatic function of IP3K-A is to phosphorylate the calcium-mobilizing second messenger Ins(1,4,5)P(3) to (Ins(1,3,4,5)P(4). Accordingly, cells overexpressing IP3K-A showed reduced calcium release and altered concentrations of InsPs, with decreasing concentrations of Ins(1,4,5)P(3), InsP(6) and Ins(1,2,3,4,5)P(5), and increasing concentrations of Ins(1,3,4,5)P(4). However, IP3K-A-induced effects on cell morphology do not seem to be dependent on enzyme activity, since a protein devoid of enzyme activity also induced the formation of branching protrusions. Therefore we propose that the morphological changes induced by IP3K-A are mediated by non-enzymatic activities of the protein.

M3 - SCORING: Zeitschriftenaufsatz

VL - 414

SP - 407

EP - 417

JO - BIOCHEM J

JF - BIOCHEM J

SN - 0264-6021

IS - 3

M1 - 3

ER -