Transgelin-3 shares homology with other cytoskeleton-interacting proteins such as transgelin and calponin. This homology suggests that Transgelin-3 may play a role in cytoskeletal dynamics and cellular motility . The protein is known to co-localize with actin and tubulin, indicating its potential involvement in maintaining the structural integrity of the cytoskeleton .
The exact biological functions of Transgelin-3 are still under investigation. However, its interaction with actin and tubulin hints at a role in neuronal plasticity or as a signaling protein . This interaction is crucial for maintaining the dynamic nature of the cytoskeleton, which is essential for various cellular processes, including cell shape, motility, and division .
Transgelin-3’s actin-binding domain allows it to interact directly with actin filaments, potentially influencing their organization and stability . The EF-hand motifs and phosphorylation sites suggest that its activity could be regulated by calcium ions and phosphorylation events, respectively . These regulatory mechanisms are vital for the protein’s function in response to cellular signals and environmental changes .
The regulation of Transgelin-3 involves multiple layers, including transcriptional control, post-translational modifications, and interactions with other cytoskeletal proteins . The presence of phosphorylation sites indicates that kinases and phosphatases may modulate its activity, thereby influencing its role in the cell .
Recombinant human Transgelin-3 is typically produced in E. coli and purified using conventional chromatography techniques . The recombinant protein often includes an N-terminal His-tag to facilitate purification and detection . It is used in various research applications to study the protein’s function, interactions, and regulatory mechanisms .