Raf1, a serine/threonine-protein kinase, is a crucial component of the RAS-activated enzymes. It initiates signaling via the MAPK cascade, thereby controlling cellular processes such as proliferation, differentiation, and survival [1].

Raf1 has diverse functions in different biological contexts. In cancer, it is involved in tumorigenesis. For instance, in Raf1-dependent cancer cells, Raf1 localizes inside mitochondria, interacts with glutaminase (GLS), and engages glutamine catabolism to support tumor growth [2]. Also, RAF1 gene fusions are recurrent driver events in infantile fibrosarcoma-like mesenchymal tumors, promoting cell proliferation and migration through constitutive upregulation of MAPK signaling [3]. In addition, in pancreatic acinar cell carcinomas, RAF1 rearrangements are relatively common, and these fusions can be identified by FISH and molecular testing [5]. Moreover, in the context of oxaliplatin-induced neuropathic pain, Raf1 interacts with OIP5 to participate in this pain mechanism [4]. In Human Cytomegalovirus (HCMV) infection, Raf1 promotes viral replication, and its activity is modulated by HCMV infection and AMPK activation [6].

In conclusion, Raf1 is essential for regulating cellular functions through the MAPK cascade. Its role in various diseases, especially cancer, is significant. Studies on Raf1 contribute to understanding disease mechanisms and may offer potential therapeutic targets for conditions like cancer, neuropathic pain, and viral infections.