Sandra Rebelo, PhD
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Affiliation(s):
Institute of Biomedicine; University of Aveiro
ORCID URL:
Areas of Interest:
Alzheimer's disease, animal models, amyloid precursor protein, ABC transporters, protein phosphorylation
Biography & Research:
Sandra Rebelo is Assistant Professor at University of Aveiro and Principal Investigator of the Institute of Biomedicine (iBiMED) of University of Aveiro. She obtained her PhD in Biochemistry from University of Aveiro with a project developed at both University of Aveiro (Prof. Odete da Cruz e Silva) and Erlangen University (Prof. Jens Wiltfang). She received a postdoctotal fellowship with a collaborative project between the Mount Sinai School of Medicine (Prof. Sam Gandy) and University of Aveiro (Prof. Odete da Cruz e Silva). She participated in 4 European projects (Biomark-APD, cNeupro, APOPIS and DIADEM) and 15 Portuguese/National projects.
Her research focuses on the molecular basis of neuropathologies such as Alzheimer’s Disease, DYT1 Dystonia and British and Danish Dementia. Principally, on protein phosphorylation dependent events, proteolytic processing and trafficking mechanisms, particularly with respect to APP, Abeta, Tau, and other proteins involved in neuropathologies. Her work allowed the identification of novel protein complexes containing protein phosphatase 1, that are regulated by the latter (i.e. APP:Fe65:PP1 and LAP1:PP1).
Recently she is studying LAP1, that is a nuclear envelope protein whose function is poorly understood, but is known to interact with torsinA - a protein central to the neurological disorder DYT1 dystonia - and also with the nuclear protein emerin which is associated with muscular dystrophies. LAP1B and LAP1C are phosphorylated at five residues (Santos et al, 2014) and Sandra Rebelo is investigating the impact of LAP1 phosphorylation on DYT1 dystonia and muscular dystrophy. LAP1 is also crucial for the maintenance of the nuclear envelope (NE) and cell cycle progression (Santos et al, 2015). Additionally, Sandra also interested on the identification of novel LAP1 interacting proteins (Serrano et al, 2016) and consequently novel LAP1 functions.
