MULIBREY Nanism

Our research focus: TRIM37, an E3 ubiquitin ligase linked to Mulibrey nanism, regulates skeletal development and cartilage integrity. We investigate the role of the protein in cartilage and chondrocytes.

Key Objectives: 

1. Map TRIM37 protein-protein interaction networks using AP-MS (Affinity Purification Mass Spectrometry) and BioID proximity labeling

2. Characterize functional consequences of TRIM37 upregulation in osteoarthritic chondrocytes

Long-term Objective:
Employ CRISPR editing to modulate TRIM37 activity and develop therapies that halt joint degradation in both Mulibrey nanism and osteoarthritis.

Want to know more about TRIM37 and mulibrey Nanism ?  

TRIM37, also known as the MULIBREY protein, is a critical factor in understanding MULIBREY nanism (muscle–liver–brain–eye syndrome). MULIBREY nanism is a rare autosomal recessive disorder that affects several tissues, primarily of mesodermal origin. It presents with severe pre- and postnatal growth failure, characteristic dysmorphic features, and normal neurological development. To date, approximately 150 cases have been documented worldwide, with a notably higher prevalence in Finland due to founder mutations.

Beyond this rare syndrome, TRIM37 has implications in a broader range of pathologies. Elevated expression of TRIM37 has been observed in various cancers, cardiovascular disorders, and, importantly, in the joints of patients with osteoarthritis. These associations highlight TRIM37's significance across diverse biological systems and diseases.

Our research aims to uncover novel interacting partners of TRIM37 in different cell types to deepen our understanding of the pathways and mechanisms it regulates. A particular focus is on its role in chondrocytes and cartilage in the context of osteoarthritis. Although we know that TRIM37 expression is increased in these cells during disease progression, it remains unclear whether this upregulation is protective or pathological. If elevated TRIM37 contributes to cartilage damage, targeting its activity could represent a therapeutic strategy to mitigate joint degradation in osteoarthritis.

By advancing our knowledge of TRIM37’s functions, we hope to uncover novel insights with broad implications for multiple diseases and fundamental cellular mechanisms.

Our review is online here