bioRxivImmunologyPreprint
E3 Ligase UBR5 HECT domain mutations in lymphoma control maturation of B cells via alternative splicing
S. A. Swenson, T. J. Gilbreath, H. Vahle, R. W. Hynes-Smith, H. C. H. Law, N. T. Woods, M. R. Green, S. M. Buckley
Abstract
Coordination of a number of molecular mechanisms including transcription, alternative splicing, and class switch recombination are required to facilitate development, activation, and survival of B cells. Disruption of these pathways can result in malignant transformation. Recently, next generation sequencing has identified a number of novel mutations in mantle cell lymphoma (MCL) patients including the ubiquitin E3 ligase UBR5. Approximately 18% of MCL patients were found to have mutations in UBR5 with the majority of mutations within the HECT domain of the protein which can accept and transfer ubiquitin molecules to the substrate. Determining if UBR5 controls the maturation of B cells is important to fully understand malignant transformation to MCL. To elucidate the role of UBR5 in B cell maturation and activation we generated a conditional mutant disrupting UBR5s C-terminal HECT domain. Loss of the UBR5 HECT domain leads to a block in maturation of B cells in the spleen and up-regulation of proteins associated with mRNA splicing via the spliceosome. Our studies reveal a novel role of UBR5 in B cell maturation by regulating alternative splicing of key transcripts during B cell development and suggests UBR5 mutations may promote mantle cell lymphoma initiation.\n\nKEY POINTSO_LIUtilizing a novel mouse model mimicking MCL patient mutations, the loss of UBR5s HECT domain causes alterations in B cell development.\nC_LIO_LIUBR5 mutations lead to stabilization of UBR5 and aberrant splicing.\nC_LI
- organism: mouse
- assay: bulk RNA-seq
- research focus: cell type annotation
- research focus: differential expression
- research focus: gene regulatory network inference
- research focus: cell signaling & trafficking
- approach: experimental assay
- approach: wet-lab / biochemical assay
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Structure of the human UBR5 E3 ubiquitin ligase
- Cryo-EM structure of the chain-elongating E3 ligase UBR5
Z. Hodakova, I. Grishkovskaya, … D. Haselbach·bioRxiv·Nov 3, 2022
- The failure of B cells to induce non-canonical MYD88 splice variants correlates with lymphomagenesis via sustained NF-κB signaling
Y. Cardona Gloria, S. H. Bernhart, … A. N. Weber·bioRxiv·Jun 18, 2020
- Lgr5-mediated restraint of β-catenin is essential for B-lymphopoiesis and leukemia-initiation
K. N. Cosgun, M. E. Robinson, … M. Mueschen·bioRxiv·Mar 12, 2020
- Interplay between UNG and AID governs intratumoral heterogeneity in mature B cell lymphoma
A. R. Ramiro, P. Delgado, … V. G. de Yebenes·bioRxiv·Jun 29, 2020
- The E3 ubiquitin ligase UBR5 regulates centriolar satellite stability and primary cilia formation via ubiquitylation of CSPP-L.
Robert F. Shearer, Kari-Anne Myrum Frikstad, … Darren N. Saunders·bioRxiv·Dec 22, 2016