Tropomodulin

Inhibition of tropomodulin capping activity leads to dramatic increase in thin filament length from its pointed end.

[5] When tropomyosin is not present Tropomodulin also assists in partially inhibiting elongation and depolymerization at the pointed filament ends.

[7] TMOD is able to have high-affinity binding through low-affinity interactions because of its ability to control subunit exchange of the pointed end of the actin filaments.

[9] Tropomodulin is a 40-kD tropomyosin-binding protein that was originally isolated from the red blood cell membrane skeleton.

[10] Known tropomodulin homologs have been identified in flies (Drosophila), worms (C.elegans), rats, chicks, and mice.

[5] Using the lab technique PCR TMOD gene was isolated and identified to have a total of 9 exons, allowing for the assumption that alternative promoters for tissue-specific expression and regulation.

Since the TMOD isoforms can influence stability of skeleton cells and regulate actin it can then be seen as essential for embryonic development.