Tropomyosin-binding properties of the CHASM protein are dependent upon its calponin homology domain

FEBS Letters
Annegret Ulke-LeméeJustin A MacDonald

Abstract

The calponin homology-associated smooth muscle protein (CHASM) can modulate muscle contractility, and its biological action may involve an interaction with the contractile filament. In this study, we demonstrate an interaction between CHASM and tropomyosin. Deletion constructs of CHASM were generated, and pull-down assays revealed a minimal deletion construct that could bind tropomyosin. Removal of the calponin homology (CH) domain or expression of the CH domain alone did not enable binding. The interaction was characterized by microcalorimetry with a dissociation constant of 2.0x10(-6) M. Confocal fluorescence microscopy also showed green fluorescent protein (GFP)-CHASM localization to filamentous structures within smooth muscle cells, and this targeting was dependent upon the CH domain.

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Citations

Mar 1, 2011·BMC Molecular Biology·Annegret Ulke-LeméeJustin A MacDonald
Apr 30, 2015·Journal of Cellular Biochemistry·Annegret Ulke-LeméeJustin A MacDonald
Jan 4, 2012·Journal of Molecular Recognition : JMR·Rajesh GhaiBrett M Collins
Jun 7, 2014·Biochimica Et Biophysica Acta·Annegret Ulke-LeméeJustin A MacDonald
Jun 2, 2020·Frontiers in Cell and Developmental Biology·Lei-Miao YinChang-Duk Jun

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