Bauereiß A, Welzel O, Jung J, Grosse-Holz S, Lelental N, Lewczuk P, Wenzel EM, Kornhuber J, Groemer TW (2015)
Publication Type: Journal article
Publication year: 2015
Book Volume: 16
Pages Range: 655-75
Journal Issue: 6
DOI: 10.1111/tra.12270
Amyloid-? (A?)-peptide, the major constituent of the plaques that develop during Alzheimer's disease, is generated via the cleavage of A? precursor protein (APP) by ?-site APP-cleaving enzyme (BACE). Using live-cell imaging of APP and BACE labeled with pH-sensitive proteins, we could detect the release events of APP and BACE and their distinct kinetics. We provide kinetic evidence for the cleavage of APP by ?-secretase on the cellular surface after exocytosis. Furthermore, simultaneous dual-color evanescent field illumination revealed that the two proteins are trafficked to the surface in separate compartments. Perturbing the membrane lipid composition resulted in a reduced frequency of exocytosis and affected BACE more strongly than APP. We propose that surface fusion frequency is a key factor regulating the aggregation of APP and BACE in the same membrane compartment and that this process can be modulated via pharmacological intervention.
APA:
Bauereiß, A., Welzel, O., Jung, J., Grosse-Holz, S., Lelental, N., Lewczuk, P.,... Groemer, T.W. (2015). Surface Trafficking of APP and BACE in Live Cells. Traffic, 16(6), 655-75. https://doi.org/10.1111/tra.12270
MLA:
Bauereiß, Anna, et al. "Surface Trafficking of APP and BACE in Live Cells." Traffic 16.6 (2015): 655-75.
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