Programmed cell death protein 11 (PDCD11)

Programmed cell death protein 11 (PDCD11) is a large, nucleolar-localized protein required for the maturation of 18S rRNA, acting through direct interaction with U3 snoRNA and containing multiple S1 RNA-binding domains and a C-terminal TPR domain[2][1]. It plays a critical regulatory role in ribosome assembly and is essential for proper rRNA processing[2][5]. Beyond its housekeeping functions, PDCD11 directly interacts with tumor suppressor p53 and E3 ligase HDM2 to facilitate p53 ubiquitination and degradation, thereby modulating the cell cycle, especially the G2/M checkpoint, and promoting cell proliferation in both p53-dependent and -independent manners[1]. PDCD11 is overexpressed in several cancers, including colorectal cancer, where it promotes tumor growth and resistance to DNA damage-induced apoptosis, highlighting its potential as a novel anti-cancer therapeutic target[1][3]. It can also bind NF-kappa-B subunits, influencing inflammatory pathways and cell differentiation, especially in neural and immune contexts[1][2]. No approved drugs are currently known to directly target PDCD11, and due to its central role in ribosome biogenesis, systemic inhibition may raise significant toxicity concerns.

Other names

Protein RRP5 homologKIAA0185NFBPALG-4RRP5NF-kappa-B-binding proteinapoptosis-linked gene 4PDCD11