Tumor protein p53-inducible nuclear protein 2 (TP53INP2)

Tumor protein p53-inducible nuclear protein 2 (TP53INP2) is a nuclear protein that shuttles between the nucleus and cytoplasm, acting as both a transcriptional coactivator (notably for various nuclear hormone receptors and ribosomal DNA transcription) and a scaffold protein essential for autophagy initiation and progression. Upon nutrient deprivation, TP53INP2 translocates to autophagic membranes, where it recruits LC3 and other Atg8 family proteins, facilitating autophagosome formation. It also plays a distinct role in death receptor signaling by promoting TRAF6-mediated K63-ubiquitination and activation of caspase-8, thereby regulating apoptosis sensitivity. TP53INP2 is implicated in cancer, muscle wasting, and metabolic disorders, with potential as a biomarker for predicting sensitivity to TRAIL-based cancer therapies. No direct pharmacological modulators targeting TP53INP2 are currently established, but its role at the intersection of autophagy and apoptosis highlights its significance in disease pathogenesis and therapeutic response[1][2][3].

Other names

C20orf110DORPINHPIG-UFLJ21759FLJ23500DKFZp434B2411DKFZp434O0827dJ1181N3.1Diabetes and obesity-regulated genep53-inducible protein Udiabetes and obesity regulated

Biomarker for predicting cancer cell response to apoptosis-inducing agents like TRAIL[3]. Scaffold-mediated enhancement of caspase-8 ubiquitination in death receptor signaling[3]. Regulation of autophagy by recruiting LC3/Atg8 family proteins to the autophagosome membrane[1][2][3].