Tetratricopeptide repeat domain 4 (TTC4)

Tetratricopeptide repeat domain 4 (TTC4) is a human protein containing tetratricopeptide repeat (TPR) motifs, which serve as scaffolds mediating protein–protein interactions[1][3][4]. TTC4 functions as a co-chaperone interacting with HSP70 and HSP90, and binds to the DNA replication initiation protein CDC6[1][3]. Identified in genomic regions linked to breast cancer and mutated in malignant melanoma, TTC4 is implicated in cancer progression[1][3]. It also participates in chromatin regulatory processes, influencing histone H4K16 acetylation in stem and cancer cells. Through interaction with TBK1, TTC4 acts as a positive regulator in the antiviral innate immune response[1]. Experimental evidence also shows that TTC4 inhibits apoptosis in vascular endothelial cells by cooperating with HSP70 and affecting lysosomal membrane stability, thus protecting against stress-induced apoptotic death[1]. Multiple transcript variants exist due to alternative splicing, and TTC4 has a broad range of functional associations driven by its role as a scaffolding, chaperone-linked protein. There are no known drugs targeting TTC4 directly, and it is not an established therapeutic target.

Other names

Tetratricopeptide repeat protein 4TTC4My044TPR repeat protein 4MGC5097FLJ41930CNS1