Recombinant Human RB1CC1 protein

RB1CC1 (RB1-inducible coiled-coil 1), also known as FIP200 (FAK family-interacting protein of 200 kDa), is a multifunctional scaffold protein critical in autophagy, cell signaling, and stress response pathways. Initially identified as a transcriptional target of the tumor suppressor RB1. it contains an N-terminal coiled-coil domain and a C-terminal Claw domain, enabling interactions with diverse partners. Its most well-characterized role is in autophagosome formation, where it acts as a core component of the ULK1 kinase complex, facilitating initiation of autophagy in response to nutrient deprivation or stress. RB1CC1 directly binds ULK1 and regulates its kinase activity, thereby coordinating autophagosome assembly.

Beyond autophagy, RB1CC1 interacts with signaling pathways such as mTOR, NF-κB, and DNA damage response networks. It modulates cell proliferation, apoptosis, and genomic stability, linking it to cancer biology. Studies highlight its dual tumor-suppressive or oncogenic roles depending on context—for example, suppressing breast cancer progression via autophagy-mediated senescence but promoting glioblastoma growth through NF-κB activation. Recombinant RB1CC1 proteins, typically produced in Escherichia coli or mammalian expression systems, are essential tools for studying its structure-function relationships, post-translational modifications, and interactions. These purified proteins enable in vitro kinase assays, binding studies, and mechanistic exploration of RB1CC1's roles in disease models. Current research focuses on targeting RB1CC1-autophagy axis for cancer therapy and neurodegenerative disorders like Alzheimer’s, where autophagy dysregulation is implicated.