RT Journal Article
T1 TRIM37 prevents formation of centriolar protein assemblies by regulating Centrobin
A1 Balestra, Fernando R.
A1 Domínguez-Calvo, Andrés
A1 Wolf, Benita
A1 Busso, Coralie
A1 Buff, Alizée
A1 Averink, Tessa
A1 Lipsanen-Nyman, Marita
A1 Huertas, Pablo
A1 Ríos, Rosa M.
A1 Gönczy, Pierre
K1 Cells
K1 Mulibrey nanism
K1 E3 ubiquitin ligase
K1 Centrioles
K1 Enzymes
K1 Células
K1 Enanismo mulibrey
K1 Ubiquitina-proteína ligasas
K1 Centriolos
K1 Enzimas
AB TRIM37 is an E3 ubiquitin ligase mutated in Mulibrey nanism, a disease with impaired organ growth and increased tumor formation. TRIM37 depletion from tissue culture cells results in supernumerary foci bearing the centriolar protein Centrin. Here, we characterize these centriolar protein assemblies (Cenpas) to uncover the mechanism of action of TRIM37. We find that an atypical de novo assembly pathway can generate Cenpas that act as microtubule-organizing centers (MTOCs), including in Mulibrey patient cells. Correlative light electron microscopy reveals that Cenpas are centriole-related or electron-dense structures with stripes. TRIM37 regulates the stability and solubility of Centrobin, which accumulates in elongated entities resembling the striped electron dense structures upon TRIM37 depletion. Furthermore, Cenpas formation upon TRIM37 depletion requires PLK4, as well as two parallel pathways relying respectively on Centrobin and PLK1. Overall, our work uncovers how TRIM37 prevents Cenpas formation, which would otherwise threaten genome integrity.
YR 2021
FD 2021-06-25
LK http://hdl.handle.net/10668/3984
UL http://hdl.handle.net/10668/3984
LA en
NO Balestra FR, Domínguez-Calvo A, Wolf B, Busso C, Buff A, Averink T, et al. TRIM37 prevents formation of centriolar protein assemblies by regulating Centrobin. Elife. 2021 Jan 25;10:e62640
DS RISalud
RD Apr 8, 2025