Tara Maisonnet
Research Subjects
Research Interests
Tara Maisonnet has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
- Lionel Berthoux
Department of Medical Biology, Université du Québec à Trois-Rivières, Trois-Rivières, QC G8Z 4M3, Canada
1 shared publication - Melodie B. Plourde
Chemistry, Biochemistry, and Physics Department, Université du Québec à Trois-Rivières, Trois-Rivières, G8Z 4M3, Canada
1 shared publication - Natacha Merindol
Université du Québec à Trois-Rivières
1 shared publication - Nour-El-Houda Hammami
Department of Medical Biology
1 shared publication - Sophie Lebel
Department of Medical Biology
1 shared publication
Latest Publications
- 1 February 2024
- Published by Canadian Science Publishing in Biochemistry and Cell Biology
- Vol. 102 (1) , 73-84
SUMO-3 promotes the ubiquitin-dependent turnover of TRIM55
Human muscle-specific RING fingers (MURFs) are members of the tripartite motif (TRIM) family of proteins characterized by their C-terminal subgroup one signature domain. MURFs play a role in sarcomere formation and microtubule dynamics. It was previously established that some TRIMs undergo post-translational modification by small ubiquitin-like modifier (SUMO). In this study, we explored the putative SUMOylation of MURF proteins as well as their interactions with SUMO. MURF proteins (TRIM54, TRIM55, and TRIM63) were not found to be SUMOylated. However, TRIM55 turnover by proteasomal and lysosomal degradation was higher upon overexpression of SUMO-3 but not of SUMO-1. Furthermore, it is predicted that TRIM55 contains two potential SUMO-interacting motifs (SIMs). We found that SIM1- and SIM2-mutated TRIM55 were more stable than the wild-type (WT) protein partly due to decreased degradation. Consistently, SIM-mutated TRIM55 was less polyubiquitinated than the WT protein, despite similar monoubiquitination levels. Using IF microscopy, we observed that SIM motifs influenced TRIM55 subcellular localization. In conclusion, our results suggest that SUMO-3 or SUMO-3-modified proteins modulate the localization, stability, and RING ubiquitin ligase activity of TRIM55.
- 1 February 2024
- Published by Canadian Science Publishing in Biochemistry and Cell Biology
- Vol. 102 (1) , 73-84
SUMO-3 promotes the ubiquitin-dependent turnover of TRIM55
Human muscle-specific RING fingers (MURFs) are members of the tripartite motif (TRIM) family of proteins characterized by their C-terminal subgroup one signature domain. MURFs play a role in sarcomere formation and microtubule dynamics. It was previously established that some TRIMs undergo post-translational modification by small ubiquitin-like modifier (SUMO). In this study, we explored the putative SUMOylation of MURF proteins as well as their interactions with SUMO. MURF proteins (TRIM54, TRIM55, and TRIM63) were not found to be SUMOylated. However, TRIM55 turnover by proteasomal and lysosomal degradation was higher upon overexpression of SUMO-3 but not of SUMO-1. Furthermore, it is predicted that TRIM55 contains two potential SUMO-interacting motifs (SIMs). We found that SIM1- and SIM2-mutated TRIM55 were more stable than the wild-type (WT) protein partly due to decreased degradation. Consistently, SIM-mutated TRIM55 was less polyubiquitinated than the WT protein, despite similar monoubiquitination levels. Using IF microscopy, we observed that SIM motifs influenced TRIM55 subcellular localization. In conclusion, our results suggest that SUMO-3 or SUMO-3-modified proteins modulate the localization, stability, and RING ubiquitin ligase activity of TRIM55.