SURP and G-patch domain-containing protein 1 (SUGP1)

SURP and G-patch domain-containing protein 1 (SUGP1) is a nuclear RNA-binding protein characterized by the presence of SURP domains and a G-patch domain, which are important for interactions with other splicing factors and RNA helicases[1][3]. SUGP1 plays a crucial role in pre-mRNA splicing, specifically involved in the selection of branch sites during the early assembly of the spliceosome. It acts as a molecular adaptor, interacting with the splicing factor SF3B1 and the DEAH-box RNA helicase DHX15. Mutations in either SUGP1 or SF3B1 disrupt this interaction, leading to aberrant RNA splicing patterns, a hallmark mechanism implicated in the development of myeloid malignancies and certain solid tumors[1][3][4]. SUGP1 is not currently recognized as a direct therapeutic target or receptor but is an essential part of the human spliceosome regulatory machinery, with its dysfunction contributing to oncogenic splicing programs in cancer. - SUGP1 mutations or disturbed interactions can recapitulate the splicing defects observed in SF3B1-mutated cancers[1][3][4]. - The C-terminal region of SUGP1 is especially critical for its interactions with SF3B1 and DHX15[1][3]. - SUGP1 is not known to interact directly with any approved drugs or to act in a manner that would make it a classic drug target[1][3][4].

Other names

SF4F23858DKFZp434E2216RBPRNA-binding protein RBPSplicing factor 4