TRIM37 recognizes a bipartite degron to ubiquitinate centrosome substrates.

TRIM37 directly ubiquitinates the centrosome-forming protein Cep192 at 7 clustered lysines near its C terminus, enabling TRIM37-dependent control of Cep192 stability.

• Why it matters: TRIM37 dysregulation is linked to tumor formation and Mulibrey nanism, yet the molecular rules for how it recognizes and ubiquitinates centrosome substrates were unclear.
• What they did: In cells and biochemical assays, TRIM37 was shown to bind Cep192 through an IDR+ASH8 region and to ubiquitinate Cep192 at 7 C-terminal lysines; IDR+ASH8 fusion to unrelated proteins promoted TRIM37-mediated degradation.
• The result: IDR+ASH8 acts as a bipartite degron: it is primarily monomeric, binds TRIM37 via two coiled-coil motifs with mid-nanomolar affinity, and its disruption increases Cep192 levels and stability.

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