Molecular cloning of a new intermediate filament protein expressed by radial glia and demonstration of alternative splicing in a novel heptad repeat region located in the carboxy-terminal tail domain.

In the present study we describe the molecular cloning of transitin, formerly named EAP-300. We show that transitin is an intermediate filament protein with a core domain most closely resembling nestin and tanabin. Transitin also contains a novel heptad amino acid repeat domain, comprising multiple leucine zipper repeats, located in its tail region. Based on these structural motifs we propose that a novel intermediate filament protein that is transiently expressed by radial glia during CNS development has been identified. We also show the existence of splice variants of transitin with splicing occurring in the novel heptad repeat domain to give rise to transitin isoforms that lack this heptad repeat. By in situ hybridization analysis we show that transitin mRNA is expressed by midline radial glial structures, by several axon commissures, and by Bergmann glia of the developing cerebelium. Based on the structural properties of the transitin protein, and expression of its mRNA, we suggest that transitin is a new member of the intermediate filament gene superfamily that is transiently expressed by radial glia.