Tiago Fleming Outeiro

 

Professor Doutor Tiago Fleming Outeiro licenciou-se em Bioquímica pela Faculdade de Ciências da Universidade do Porto e concluiu o seu doutoramento em 2004 no MIT, USA. Fez o seu PhD na farmacêutica americana FoldRX e foi, desde 2007, principal investigador e líder de grupo no Instituto de Medicina Molecular em Lisboa, durante 3 anos.
Ao longo da sua carreira conta com várias publicações, algumas patentes e com vários prémios dos quais: Junior Faculty Award, AD/PD Meeting, Prague, Czech Republic; Best Scientific Article in 2007, Portuguese Society for Neuroscience; Marie Curie International Reintegration Grant, European Commission; Massachusetts Biomedical Research Corporation, Tosteson Award, Postdoctoral Fellowship, entre tantos outros.
Atualmente é professor catedrático e diretor do departamento de Investigação de Neurodegeneração na University Medical Center Göttingen, Alemanha, e ainda professor auxiliar no Instituto de Fisiologia da Faculdade de Medicina da Universidade de Lisboa.

 

The baker, sugar, and the molecular basis of Parkinson's disease

Aggregation of alpha-synuclein (ASYN) in Lewy bodies and Lewy neurites is the typical pathological hallmark of Parkinson’s disease (PD) and other synucleinopathies. Furthermore, mutations in the gene encoding for ASYN are associated with familial and sporadic forms of PD, suggesting this protein plays a central role in the disease. However, the precise contribution of ASYN to neuronal dysfunction and death is unclear. There is intense debate on the nature of the toxic species of ASYN, and little is still known about the molecular determinants of oligomerization and aggregation of ASYN in the cell. Using the budding yeast as a living test tube, we are making progress towards the understanding of the basic molecular mechanisms underlying PD and other synucleinopathies. In order to clarify the effects of different posttranslational modifications on the toxicity and aggregation of ASYN, we employ a variety of model systems. Phosphorylation and glycation are emerging as important modifications affecting ASYN aggregation. Altogether, our data shed light into the molecular underpinnings of PD, and open novel perspectives for therapeutic intervention in synucleinopathies.