It is known that aberrant LLPS disrupts signaling pathways that curb tumor growth. For example, the FERM domain protein Merlin, which is encoded by the NF2 gene, is a known tumor suppressor protein whose main function is to regulate intracellular signaling pathways and to facilitate innate immunity against cancer by minimizing oncogene expression. However, when Merlin is inactivated due to promoter methylation in schwannomas, it becomes mutated in the NF2 gene and can phase separate upon binding with the interferon regulatory factor 3 protein. The resulting condensates then suppress the cGAS-STING signaling pathway (which typically inhibits tumor formation), resulting in potential tumorigenesis. Cancer proliferation can also be regulated through the non receptor protein tyrosine phosphatase encoded by PTPN11, i.e., SHP2, which is instrumental in regulating the RAS-MAPK signal transduction process (which itself regulates oncogenesis) and organism development in general. SHP2 mutations can result in condensation via LLPS, leading to significant accumulation of wild-type SHP2 within the condensate itself and depleting the cell of SHP2 capable of regulating RAS-MARK, thus resulting in potential tumorigenesis. Finally, while biological LLPS is typically limited to nucleic acids and proteins/peptides, other types of cellular biomolecules can phase separate, such as glycogen. Glycogen typically accumulates in liver cells, but glucose-6-phosphatase (G6PC) hydrolyzes excess glycogen. However, in some pre-malignant cells, G6PC function is downregulated, leading to glycogen accumulation. This accumulated glycogen can phase separate, resulting in sequestration of a known tumor suppressor Mst1/2