E3 ubiquitin-protein ligase TRIM58 (TRIM58)

E3 ubiquitin-protein ligase TRIM58 (TRIM58) is a member of the tripartite motif (TRIM) protein family and functions as an E3 ubiquitin ligase that mediates the ubiquitin-dependent proteasomal degradation of substrate proteins—including the dynein motor complex during erythroblast maturation[1][2][3]. TRIM58 is specifically induced during late erythropoiesis and is essential for normal nuclear polarization and enucleation of erythroblasts, thus regulating red blood cell formation. Genome-wide association studies implicate TRIM58 in human erythrocyte traits. In cancer biology, TRIM58 can act as a tumor suppressor, notably in colorectal cancer, by promoting the ubiquitination and degradation of targets such as RECQL4 and β-catenin, thereby modulating cell cycle regulation, AKT signaling, cell proliferation, and apoptosis[5][6]. TRIM58 dysfunction or downregulation is associated with malignancies and hematological disorders, marking it as a target of interest for future therapies, though no drugs are currently approved to modulate its activity.

Other names

Protein BIA2RING-type E3 ubiquitin transferase TRIM58Tripartite motif-containing protein 58BIA2

Polyubiquitination and proteasomal degradation of target proteins (e.g., dynein intermediate chains, RECQL4, β‐catenin); this leads to regulation of cell cycle progression, cell proliferation, apoptosis, and nuclear events in erythropoiesis