Ribosome quality control complex subunit NEMF (NEMF)

Ribosome quality control complex subunit NEMF is a protein that binds to stalled 60S ribosomal subunits and recognizes aberrant nascent polypeptide chains attached to tRNA[1][3][4]. Upon ribosomal stalling, NEMF recruits the E3 ubiquitin ligase Listerin (LTN1), promoting the ubiquitination and subsequent degradation of the defective nascent chains, thus preserving cellular proteostasis[3]. NEMF also mediates CAT tailing—extension of stalled chains with non-templated C-terminal alanines—which facilitates their recognition and degradation[3]. Functionally, NEMF is vital in neurons, with loss-of-function mutations leading to neurodegeneration, motor neuropathy, and intellectual disability in humans and mice[2][3]. In Drosophila, its homolog has tumor suppressor activity[1]. There is currently no evidence for direct drug targeting, biomarkers, or major safety concerns associated with NEMF modulation. NEMF is not a receptor, enzyme, or transporter, but a critical protein in ribosome quality control[1][3][4]. Mutations in NEMF cause neurodevelopmental and neurodegenerative disorders[2][3]. NEMF's mechanism centers on protein surveillance, not on classical signaling pathways or drug interactions[1][3].

Other names

nuclear export mediator factorNEMFSDCCAG1NY-CO-1FLJ10051RQC2Antigen NY-CO-1Serologically defined colon cancer antigen 1caliban homolog (Drosophila)IDDSAPN