Zooming into protein oligomerization in neurodegeneration using BiFC.
Several neurodegenerative diseases are characterized by the accumulation of misfolded and aggregated proteins, which lead to neurotoxicity. However, the nature of those toxic species is controversial. Developments in optical microscopy and live-cell imaging are essential in providing crucial insight into the molecular mechanisms involved. In particular, the technique of bimolecular fluorescence complementation (BiFC) represents a remarkable improvement for observing protein-protein interactions within living cells. Unlike other techniques, BiFC provides spatial and temporal resolution and can be carried out in a physiological environment. Among other applications, BiFC has been used to study molecular determinants of oligomerization in neurodegenerative disorders, thereby promising to unveil novel targets for therapeutics. We review the applicability of BiFC for investigating the molecular basis of neurodegenerative diseases associated with protein misfolding and aggregation.
Gonçalves
Susana A
SA
Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal.
Matos
Joana E
JE
Outeiro
Tiago F
TF
D000818:Animals; D006801:Humans; D008164:Luminescent Proteins / Q000032:analysis* / Q000378:metabolism; D009474:Neurons / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D055503:Protein Multimerization; D011506:Proteins / Q000032:analysis* / Q000378:metabolism*
D008164:Luminescent Proteins; D011506:Proteins