Cct7, also known as chaperonin containing TCP-1 subunit eta, is a member of the TCP1 chaperone family. It is involved in cytoskeletal protein folding and unfolding, and is a subunit of the essential eukaryotic chaperonin TRiC/CCT complex, which has a role in the folding of various proteins [5,3]. CCT7 may participate in multiple biological processes such as sperm flagella development, viral replication, and the regulation of GPCR expression, and is related to diseases like endometrial cancer, hepatocellular carcinoma, and drug-resistant epilepsy [1,2,6,5,7,8].

Deletion of the germ cell-specific co-factor Styxl1, which interacts with CCT7, leads to male infertility and microtubule defects in sperm flagella, revealing the role of CCT7 in sperm flagella development [1]. In fowl adenovirus serotype 4 (FAdV-4) infection, knockdown of cellular CCT7 by RNAi reduces the expression of the viral hexon protein and suppresses viral replication, suggesting CCT7 is required for FAdV-4 replication [2]. In canine parvovirus (CPV) replication, knocking down CCT7 expression by RNA interference reduces the expression level of the viral VP2 protein, indicating CCT7 is involved in CPV replication [4]. In endometrial cancer, suppression of CCT7 induced a function loss in Ishikawa and RL95-2 cells, suggesting CCT7 may be involved in the development of endometrial cancer by promoting myometrial invasion or metastasis [5].

In conclusion, CCT7 is crucial for protein folding and has diverse functions in biological processes. Its role in diseases such as viral infections and cancers has been revealed through gene-knockdown experiments. Understanding CCT7 can provide insights into the mechanisms of these diseases and potential therapeutic targets.