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Updated: May 7, 2026

From a 2DE-Gel Spot to Protein Function: Lesson Learned From HS1 in Chronic Lymphocytic Leukemia
Published on: October 19, 2014
RING finger protein family in leukemia (Review)
Ye Wang1, Yue Zhao2, Jihong Zhang2
1Department of Pediatrics, Shengjing Hospital of China Medical University, Shenyang, Liaoning 110022, P.R. China.
Abstract:
Ubiquitination is a highly conserved and indispensable post‑translational modification in eukaryotic systems, serving as a fundamental regulatory mechanism for protein homeostasis and function. The RING finger protein (RNF) family, distinguished by their characteristic RING domains, constitute a major class of E3 ubiquitin ligases that orchestrate substrate specificity and ubiquitin transfer, thereby modulating diverse cellular processes. Accumulating evidence over the past decade has firmly established the pivotal involvement of RNF proteins in various pathological conditions, including infectious diseases, autoimmune disorders and malignancies. The present review systematically examined the mechanistic contributions of RNF family members to leukemogenesis, with particular emphasis on their regulatory roles in disease progression and therapeutic resistance. By synthesizing current knowledge, it highlighted the emerging potential of RNF proteins as both prognostic biomarkers and therapeutic targets in leukemia and advocate for the development of selective RNF‑targeting inhibitors as a promising strategy for leukemia treatment.

