Diversification of the calponin family proteins by gene amplification and repeat expansion of calponin-like motifs

The calponin family proteins in vertebrates, including calponin and transgelin (also known as SM22 or NP25), regulate actin-myosin interaction and actin filament stability and are involved in regulation of muscle contractility and cell migration. Related proteins are also present in invertebrates and fungi. Animals have multiple genes encoding calponin family proteins with variable molecular features, which are often expressed in the same tissues or cells. However, functional studies of this class of proteins have been reported only in limited species. Through database searches, I found that the calponin family proteins were diversified in animals by gene amplification and repeat expansion of calponin-like (CLIK) motifs, which function as actin-binding sequences. Transgelin-like proteins with a single CLIK motif are the most primitive type and present in fungi and animals. In many animals, additional calponin family proteins containing multiple CLIK motifs, as represented by vertebrate calponins with three CLIK motifs, are present. Interestingly, in several invertebrate species, there are uncharacterized calponin-related proteins with highly expanded repeats of CLIK motifs (up to 23 repeats in mollusks). These variable molecular features of the calponin family proteins may be results of evolutionary adaptation to a broad range of cell biological events.

Automated summary

The calponin family proteins play important roles in vertebrates, regulating actin-myosin interaction and actin filament stability, and are involved in muscle contraction and cell migration. These proteins have diversified in animals through gene amplification and repeat expansion of calponin-like motifs, resulting in variable molecular features.