Muscle-specific RING finger protein 2 (MuRF2) (MuRF2)

MuRF2 (Muscle-specific RING finger protein 2), also known as TRIM55, is a striated muscle-specific E3 ubiquitin ligase that plays a critical role in maintaining muscle protein homeostasis and structural integrity. It belongs to the tripartite motif (TRIM) family and is primarily expressed in skeletal and cardiac muscle, where it regulates the turnover of sarcomeric proteins and the activity of key transcription factors like serum response factor (SRF) and peroxisome proliferator-activated receptors (PPARs). MuRF2 is involved in the early stages of myofibrillogenesis and microtubule stabilization, making it essential for proper muscle development and adaptation to mechanical stress. In disease states, MuRF2 is implicated in muscle atrophy, cardiac cachexia, and diabetic cardiomyopathy, where its dysregulation contributes to protein degradation and metabolic dysfunction. Additionally, MuRF2 has been identified as a potential tumor suppressor or promoter in various cancers, such as hepatocellular carcinoma and lung adenocarcinoma, depending on the cellular context. While no drugs are currently approved specifically for MuRF2, it is an emerging therapeutic target for treating muscle-wasting conditions and heart failure, with research focusing on experimental small-molecule inhibitors like ID#704946 and MyoMed-205 that can modulate its ligase activity or its interactions with substrate proteins.

Other names

TRIM55Tripartite motif-containing protein 55RNF209Muscle-specific RING finger 2

Inhibition of E3 ubiquitin ligase activity and disruption of protein-protein interactions with substrate proteins or E2 conjugating enzymes.