Cct7, also known as chaperonin containing TCP-1 subunit eta, is a subunit of the TRiC/CCT complex. This complex is essential for cytoskeletal protein folding and unfolding. CCT7 is involved in pathways related to protein folding and may play a role in maintaining proper cellular function. Genetic models can be valuable for studying its function in more detail [1,3,5].

Deletion of Styxl1, a germ cell-specific co-factor of the CCT complex, leads to male infertility and sperm flagella microtubule defects. The N-terminal rhodanese-like domain of STYXL1 interacts with CCT7, among other CCT complex subunits, and Styxl1 deletion causes CCT complex assembly and tubulin polymerization defects, 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, indicating CCT7 is required for FAdV-4 replication [2].

In canine parvovirus (CPV) replication, CCT7 interacts with the viral VP2 protein, improves VP2 protein stability, and its knockdown reduces VP2 protein expression, suggesting CCT7's involvement in CPV replication [4].

In endometrial cancer, CCT7 expression is higher in cancer tissues compared to adjacent normal tissues, and its suppression in Ishikawa and RL95-2 cells induces function loss, potentially contributing to endometrial cancer development and metastasis [5].

In conclusion, CCT7 is crucial for protein folding processes, especially in relation to sperm flagella development, viral replication, and endometrial cancer progression. The use of gene knockout models in these studies has been instrumental in revealing the role of CCT7 in these specific biological processes and disease conditions.