My previous research experience has been obtained studying two aspects of the protein degradation machinery. In Rosine Haguenauer-Tsapis’ laboratory, I worked on the role of Lys63-linked ubiquitin chains in the MVB sorting of membrane proteins in the endocytic pathway. In Prof. Per Ljungdahl’s laboratory, I focused on the protein quality control mediated by the Ubiquitin Proteasome System. More specifically, I studied the function and turnover of three inner nuclear membrane (INM) proteins comprising the ASI complex. The projects I was involved in during my studies were formatted into five manuscripts published in scientific journals among them a publication in ´´Nature’’, where we designated a novel degradative pathway INMAD, i.e. INM associated degradation, which is functionally required to maintain and safeguard the integrity of the INM. The last five years, as a post-doctoral fellow in Prof. Leonidas Stefanis laboratory at BRFAA, I have focused my research interests on understanding how cellular protein degradative processes and Parkinson’s Disease (PD) are coupled. I have developed a novel cell system enabling us to follow α-Synuclein (α-Syn) aggregation and degradation, a work supported by Innovative Medicines Initiative 2 and published last year in the Journal of Neurochemistry. Currently, I am working on endocytosis of exosomes loaded with α-Syn, the degradation process involved and the subsequent release through exosomes in neuronal and glial cells, a project supported by NSRF (2nd Call for the support of PostDoc Researchers).