Key result
The calponin homology-associated smooth muscle protein (CHASM) interacts with tropomyosin with a dissociation constant of 2.0x10(-6) M, and this interaction is dependent upon its CH domain.
Effect estimate: dissociation constant of 2.0x10(-6) M
The CHASM protein interacts with tropomyosin and localizes to smooth muscle filaments in a calponin homology domain-dependent manner.
CHASM-tropomyosin binding is hypothesis-generating for smooth muscle regulation; leaves open any cardiovascular disease relevance.
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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Ulke‐Lemée et al. (2010) studied this question. CHASM protein constructs was evaluated on Interaction between CHASM and tropomyosin (dissociation constant of 2.0x10(-6) M). The calponin homology-associated smooth muscle protein (CHASM) interacts with tropomyosin with a dissociation constant of 2.0x10(-6) M, and this interaction is dependent upon its CH domain.
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