Area of research
Molecular Biology · Public Health, Environmental and Occupational Health
Research interest
Research topics from publications: Regulation of misfolded protein aggregation and degradation by SUMOylation in budding yeast; A distinct isoform of Msp300 (nesprin) organizes the perinuclear microtubule-organizing center in adipocytes. Representative work: ) causes Huntington's disease. Protein fragments of Htt exon 1 with polyQ expansion (mutant HTT, mHtt) are prone to aggregation, resulting in oligomers, amyloid fibrils, or large inclusion bodies. Previous studies demonstrate mHtt SUMOylation, a process of covalent attachment of small ubiquitin-like modifiers (SUMO) to target proteins. Protein polySUMOylation further triggers its ubiquitination and segregation by the polySUMO axis. Here, we examined how SUMOylation regulates aggregation and degradation of Htt103QP-GFP, a model mHtt, in budding yeast. We first confirmed Htt103QP-GFP SUMOylation in budding yeast. We also found that recruitment of the SUMO E2-conjugating enzyme to Htt103QP-GFP In many cell types, disparate noncentrosomal microtubule-organizing centers (ncMTOC) replace functional centrosomes and serve the unique needs of the cell types in which they form. In Drosophila fat body cells, an ncMTOC is organized on the nuclear surface. This perinuclear ncMTOC is anchored by the nesprin Msp300. Msp300 and the spectraplakin short stop (shot) are codependent for localization to the nuclear envelope to generate the ncMTOC, where they recruit the microtubule (MT) minus-end stabilizer Patronin (CAMSAP). The Msp300 gene is complex, encoding at least 11 isoforms. Here, we show that two Msp300 isoforms, Msp300-PE and -PG, are required and one, Msp300-PE, appears sufficient to ge