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Smoothelin contains a novel actin cytoskeleton localization sequence with similarity to troponin T.

Quensel, Christina and Krämer, Jochen and Cardoso, M Cristina and Leonhardt, Heinrich (2002):
Smoothelin contains a novel actin cytoskeleton localization sequence with similarity to troponin T.
In: Journal of cellular biochemistry, pp. 403-9, 85, (2), ISSN 0730-2312,
[Online-Edition: http://www.cardoso-lab.org/publications/Quensel_2002.pdf],
[Article]

Abstract

Smoothelin, a cytoskeletal protein, exists in a large isoform specifically expressed in vascular smooth muscle cells, and a small visceral isoform generated by a downstream transcriptional start site. Using fusions to the green fluorescent protein, we could show that both smoothelin isoforms are localized at actin containing filaments and mapped two domains that are each sufficient for localization at the actin cytoskeleton. The first domain is located in the vascular-specific, N-terminal half of smoothelin and the second in the common, C-terminal half. The second domain shares clear sequence similarity with a domain of troponin T involved in actin filament association. These results suggest that the tissue-specific expression of smoothelin isoforms might contribute to the different contractile properties of smooth muscle cells.

Item Type: Article
Erschienen: 2002
Creators: Quensel, Christina and Krämer, Jochen and Cardoso, M Cristina and Leonhardt, Heinrich
Title: Smoothelin contains a novel actin cytoskeleton localization sequence with similarity to troponin T.
Language: German
Abstract:

Smoothelin, a cytoskeletal protein, exists in a large isoform specifically expressed in vascular smooth muscle cells, and a small visceral isoform generated by a downstream transcriptional start site. Using fusions to the green fluorescent protein, we could show that both smoothelin isoforms are localized at actin containing filaments and mapped two domains that are each sufficient for localization at the actin cytoskeleton. The first domain is located in the vascular-specific, N-terminal half of smoothelin and the second in the common, C-terminal half. The second domain shares clear sequence similarity with a domain of troponin T involved in actin filament association. These results suggest that the tissue-specific expression of smoothelin isoforms might contribute to the different contractile properties of smooth muscle cells.

Journal or Publication Title: Journal of cellular biochemistry
Volume: 85
Number: 2
Divisions: 10 Department of Biology > Cell Biology and Epigenetics
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10 Department of Biology
Date Deposited: 06 Mar 2010 07:22
Official URL: http://www.cardoso-lab.org/publications/Quensel_2002.pdf
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