NUFIP2 (F5O7H) Rabbit mAb #10893

Nuclear FMR1-interacting protein 2 (NUFIP2) was initially identified and characterized as a novel RNA-binding protein associated with the fragile X mental retardation protein (FMRP) (1). NUFIP2 functions as a ribonucleoprotein large subunit assembly factor and facilitates ribosome biogenesis through binding of specific components necessary for protein synthesis (1). As one of many FMRP-interacting proteins, NUFIP2 localizes to several subcellular compartments, including the cytoplasmic stress granule, nuclear body, and ribosome, indicating involvement in both nuclear and cytoplasmic processes (2). Moreover, the subcellular distribution of NUFIP2 is cell cycle-dependent in cultured cells, suggesting that the composition of FMRP-containing RNP complexes may be cell cycle-modulated (1). Under lysosomal-damaging conditions, NUFIP2 directly interacts with GABARAPs of the ATG8 family. Subsequent Atg8ylation of NUFIP2 drives its recruitment to stress granules where it contributes to mTOR inactivation via the Ragulator–RagA/B complex (3,4). NUFIP2 has also been identified as a regulatory cofactor of Roquin-1 and Roquin-2, RNA-binding proteins which recognize secondary structures in target mRNA 3′-UTRs and induce mRNA decay (5).