Identification and functional characterization of an aggregation domain in long myosin light chain kinase

The FEBS Journal
Wen Cheng ZhangMin Sheng Zhu

Abstract

The functions of long smooth muscle myosin light chain kinase (L-MLCK), a molecule with multiple domains, are poorly understood. To examine the existence of further potentially functional domains in this molecule, we analyzed its amino acid sequence with a tango program and found a putative aggregation domain located at the 4Ig domain of the N-terminal extension. To verify its aggregation capability in vitro, expressible truncated L-MLCK variants driven by a cytomegalovirus promoter were transfected into cells. As anticipated, only the overexpression of the 4Ig fragment led to particle formation in Colon26 cells. These particles contained 4Ig polymers and actin. Analysis with detergents demonstrated that the particles shared features in common with aggregates. Thus, we conclude that the 4Ig domain has a potent aggregation ability. To further examine this aggregation domain in vivo, eight transgenic mouse lines expressing the 4Ig domain (4Ig lines) were generated. The results showed that the transgenic mice had typical aggregation in the thigh and diaphragm muscles. Histological examination showed that 7.70 +/- 1.86% of extensor digitorum longus myofibrils displayed aggregates with a 36.44% reduction in myofibril diameter, where...Continue Reading

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Citations

Apr 12, 2011·Molecular Biotechnology·Juanmin ZhaWeiqi He
Nov 17, 2009·Journal of Bacteriology·Takahiro NonakaMakoto Miyata
Mar 27, 2018·Biochemical and Biophysical Research Communications·Jirong JiaWensheng Li

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