2024 | Alessandro Ianni, Poonam Kumari, Shahriar Tarighi, Thomas Braun and Alejandro Vaquero
SIRT7 is a unique sirtuin enzyme that plays a critical role in cancer development and progression. It is primarily localized in the nucleolus, where it regulates ribosome biogenesis and maintains genomic stability by preventing homologous recombination of rDNA sequences. SIRT7 also interacts with various proteins involved in ribosome biogenesis and influences mRNA processing and translation. Additionally, SIRT7 exhibits RNA-binding capabilities, which may influence RNA stability and translation efficiency. It also has distinct catalytic activities, including deacetylation and deacylase functions, which can impact gene expression and chromatin regulation. SIRT7's role in cancer is context-dependent, with pro-tumorigenic and tumor-suppressive functions depending on the cellular environment. In some cancers, SIRT7 promotes cell proliferation by enhancing ribosome biogenesis, while in others, it represses the expression of ribosomal proteins and influences mRNA translation. SIRT7 also plays a role in the nucleolar stress response, which is crucial for cellular adaptation to stress. In addition, SIRT7 is involved in the regulation of the immune response by modulating the expression of PD-L1, a molecule that helps cancer cells evade immune surveillance. SIRT7's functions in various cancers, including liver, pancreatic, gastric, colorectal, skin, lung, thyroid, gynecologic, prostate, bladder, and sarcoma cancers, are complex and context-dependent. SIRT7's ability to modulate signaling pathways such as AKT and TGF-β, as well as its interactions with other proteins, highlights its potential as a therapeutic target for cancer treatment. Overall, SIRT7's multifaceted roles in cancer development and progression make it a promising target for personalized cancer therapies.SIRT7 is a unique sirtuin enzyme that plays a critical role in cancer development and progression. It is primarily localized in the nucleolus, where it regulates ribosome biogenesis and maintains genomic stability by preventing homologous recombination of rDNA sequences. SIRT7 also interacts with various proteins involved in ribosome biogenesis and influences mRNA processing and translation. Additionally, SIRT7 exhibits RNA-binding capabilities, which may influence RNA stability and translation efficiency. It also has distinct catalytic activities, including deacetylation and deacylase functions, which can impact gene expression and chromatin regulation. SIRT7's role in cancer is context-dependent, with pro-tumorigenic and tumor-suppressive functions depending on the cellular environment. In some cancers, SIRT7 promotes cell proliferation by enhancing ribosome biogenesis, while in others, it represses the expression of ribosomal proteins and influences mRNA translation. SIRT7 also plays a role in the nucleolar stress response, which is crucial for cellular adaptation to stress. In addition, SIRT7 is involved in the regulation of the immune response by modulating the expression of PD-L1, a molecule that helps cancer cells evade immune surveillance. SIRT7's functions in various cancers, including liver, pancreatic, gastric, colorectal, skin, lung, thyroid, gynecologic, prostate, bladder, and sarcoma cancers, are complex and context-dependent. SIRT7's ability to modulate signaling pathways such as AKT and TGF-β, as well as its interactions with other proteins, highlights its potential as a therapeutic target for cancer treatment. Overall, SIRT7's multifaceted roles in cancer development and progression make it a promising target for personalized cancer therapies.