RB1-inducible coiled-coil protein 1 (RB1CC1)

RB1-inducible coiled-coil protein 1 (RB1CC1, also known as FIP200) is a multifunctional protein that regulates autophagy, cell cycle progression, cell proliferation, apoptosis, and cell migration[1][2][4]. It is a central component of the ULK1 autophagy initiation complex, acting as a scaffold for interactions with proteins such as ATG13 and ULK1/2, and is crucial for autophagosome formation in response to cellular and metabolic cues[1][2]. In the nucleus, RB1CC1 functions as a tumor suppressor by promoting RB1 gene transcription and inhibiting oncogenic pathways including PYK2/TAZ/PD-L1 signaling[3][1]. Reduced expression or mutation of RB1CC1 is associated with tumor progression and worse outcomes in cancers such as renal cell carcinoma and breast cancer, and it has both prognostic and potential predictive biomarker value. Therapeutic strategies targeting RB1CC1 activity may sensitize tumors to immunotherapy by reducing PD-L1-mediated immune evasion[3]. It also has reported roles in development, cellular differentiation, and the regulation of response to DNA damage.

Other names

FIP200KIAA0203RBICCCc1DRAGOU14ATG17PPP1R131FAK family kinase-interacting protein of 200 kDa200 kDa FAK family kinase-interacting proteinphosphatase 1 regulatory subunit 131CC1

Inhibition or enhancement of autophagy (via ULK complex), Tumor suppression by inhibition of PYK2/TAZ/PD-L1 signaling, Regulation of RB1 transcription, Enhancement of immunotherapy efficacy by suppression of PD-L1 expression