Anti-TRIM37/MUL antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

TRIM37 also known as MUL is an E3 ubiquitin-protein ligase with a molecular mass of approximately 130 kDa. This protein plays a role in the ubiquitination process which involves labeling proteins for degradation by the proteasome. TRIM37 is widely expressed in various tissues with higher levels seen in the brain liver and heart. The protein contains a RING domain which is important for its ligase activity and mediates the attachment of ubiquitin molecules to substrate proteins therefore controlling the stability and turnover of various cellular proteins.

Biological function summary

TRIM37 regulates processes that are important for cell growth and division as well as for maintaining cellular homeostasis. It functions as part of a larger complex involved in the ubiquitin-proteasome pathway which helps to control protein degradation and recycling within the cell. Through its role in ubiquitination TRIM37 modulates the levels of proteins that are critical for controlling cell cycle progression and responding to stress. Additionally TRIM37 is involved in organizing centrosomes structures that play an important role in chromosome segregation during cell division.

Pathways

TRIM37 interacts with cellular pathways controlling autophagy and the DNA damage response. It contributes to autophagy by regulating proteins that control the formation and clearance of autophagosomes such as ULK1. In the DNA damage response TRIM37 modulates repair processes by regulating the stability of proteins like FANCD2 which is involved in the repair of DNA crosslinks. This illustrates how TRIM37 fits into wider networks inside the cell and influences processes important for maintaining genome integrity.

Associated diseases and disorders

TRIM37 mutations are linked with Mulibrey nanism a rare growth disorder characterized by multi-organ fibrosis and growth failure. Abnormal functioning of TRIM37 disrupts the regulation of cellular proteins that maintain organ size and structure. Furthermore TRIM37 may play a role in the development of some cancers including breast cancer. In this context the protein can influence cancer progression by modifying the stability of oncogenes or tumor suppressors such as p53 adding further complexity to how TRIM37 impacts disease states.