TRIM37 (Tripartite motif containing 37) restricts centriole reduplication during centriole biogenesis. It participates in epigenetic transcriptional repression by facilitating monoubiquitination of ′Lys-119′ of histone H2A (H2AK119Ub). TRIM37 also possesses anti-HIV activity. Mutation in TRIM37 causes an autosomal recessive prenatal-onset growth disorder, mulibrey nanism with dysmorphic features, cardiomyopathy, and hepatomegaly.
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Centrioles are essential for forming cilia, flagella, and centrosomes and are thus critical for a range of fundamental cellular processes. Despite their importance, the mechanisms governing centriole biogenesis remain incompletely understood. We performed a high-content genome-wide small-interfering-RNA-based screen to identify
The Journal of general virology, 95(Pt 4), 960-967 (2013-12-10)
Trim 5α was the first member of the tripartite motif (TRIM) family of proteins that was identified to potently restrict human immunodeficiency virus type 1 (HIV-1) replication. The breadth of antiretroviral activity of TRIM family members is an active area
Mulibrey nanism is an autosomal recessive prenatal-onset growth disorder characterized by dysmorphic features, cardiomyopathy, and hepatomegaly. Mutations in TRIM37 encoding a tripartite motif (TRIM, RING-B-box-coiled-coil)-family protein underlie mulibrey nanism. We investigated the ubiquitin ligase activity predicted for the RING domain
The TRIM37 (also known as MUL) gene is located in the 17q23 chromosomal region, which is amplified in up to ∼ 40% of breast cancers. TRIM37 contains a RING finger domain, a hallmark of E3 ubiquitin ligases, but its protein
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