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Official PDF TranslationActa Biochimica et Biophysica Sinica

RNF126 writes a non-canonical ubiquitin code on midnolin to tune protein stability

Authors: Yun Yang; Jin Ren; Xiang Qiu; Yanlin Liu; Shilin Yuan; Ronggui Hu; Zhixiong Xia; Chuanyin Li

DOI: 10.3724/abbs.2025232Status: Verified Translated Edition
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Key Findings in This Report

• RNF126 is identified as the E3 ubiquitin ligase for MIDN, catalyzing its ubiquitination at non-canonical cysteine, serine, and threonine residues. • Non-lysine ubiquitination of MIDN targets it for 26S proteasomal degradation, revealing a novel regulatory mechanism. • The RNF126-MIDN axis controls EGR1 abundance, thereby modulating tumor-suppressor proteins PTEN and p53. • The RNF126-MIDN ubiquitination cascade represents a potential therapeutic target in testicular germ-cell tumors (TGCTs).