Premium
Smoothelin contains a novel actin cytoskeleton localization sequence with similarity to troponin T
Author(s) -
Quensel Christina,
Krämer Jochen,
Cardoso Maria Cristina,
Leonhardt Heinrich
Publication year - 2002
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.10143
Subject(s) - gene isoform , actin , cytoskeleton , microbiology and biotechnology , actin cytoskeleton , lim domain , biology , chemistry , cell , biochemistry , gene , transcription factor , zinc finger
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. J. Cell. Biochem. 85: 403–409, 2002. © 2002 Wiley‐Liss, Inc.