Literature DB >> 11948695

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

Christina Quensel1, Jochen Krämer, Maria Cristina Cardoso, Heinrich Leonhardt.   

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. Copyright 2002 Wiley-Liss, Inc.

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Year:  2002        PMID: 11948695     DOI: 10.1002/jcb.10143

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  2 in total

1.  The role of the calponin homology domain of smoothelin-like 1 (SMTNL1) in myosin phosphatase inhibition and smooth muscle contraction.

Authors:  Meredith A Borman; Tiffany A Freed; Timothy A J Haystead; Justin A Macdonald
Journal:  Mol Cell Biochem       Date:  2009-02-14       Impact factor: 3.396

2.  Smoothelin-positive cells in human and porcine semilunar valves.

Authors:  Massimo Cimini; Kem A Rogers; Derek R Boughner
Journal:  Histochem Cell Biol       Date:  2003-10-02       Impact factor: 4.304

  2 in total

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