25-30 August 2019
Henry Ford Building
Europe/Berlin timezone

Mechanistic insight in the role of SUMO in α-Synuclein aggregation

Not scheduled
Harnack House and Henry Ford Building

Harnack House and Henry Ford Building

Board: 352
Poster Posters


Ms Rajlaxmi Panigrahi (I.I.T Bombay)


Intrinsically disordered presynaptic neuronal protein, α-Synuclein plays a critical role in synaptic vesicle trafficking, though the exact mechanism still remains unknown. It is also amyloidogenic in nature and deposits of higher aggregates of α-Synuclein in the Lewy bodies are the histopathological hallmark of second most prevalent neurodegenerative disorder, Parkinson’s disease. Posttranslational modifications α-synuclein such as ubiquitination, phosphorylation and nitrosylation, play a crucial role in modulation of α-synuclein aggregation kinetics. SUMOylation, a post-translational modification involving covalent attachment of SUMO to the target protein has been shown to abolish α-synuclein fibril formation. In our study, we showed that SUMO-1 interacts non-covalently with α-synuclein and alters the aggregation kinetics of α-Synuclein by using ThT fluorescence, circular dichroism, nuclear magnetic resonance spectroscopy and atomic force microscopy. Interaction with SUMO results in the delayed aggregation rate of α-Synuclein. The residues specific interaction studied by solution state NMR reveals that, SUMO1 interacts to the protein in the N-terminal region which has been previously shown to form a β-hairpin loop structure which upon sequestration completely inhibits α-Synuclein aggregation. This study gives a better insight about the SUMO and Synuclein interaction and may suggest a new signaling or regulatory mechanism of SUMO in Parkinson’s disease.

Primary authors

Ms Rajlaxmi Panigrahi (I.I.T Bombay) Mr Jai Shankar Singh (I.I.T Bombay) Mr Dev Thacker (I.I.T Bombay) Dr Priyatosh Ranjan (I.I.T Bombay) Prof. Ashutosh Kumar (I.I.T Bombay)

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