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Cited 19 time in webofscience Cited 21 time in scopus
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Polo-like kinase 2 phosphorylation of amyloid precursor protein regulates activity-dependent amyloidogenic processing

Authors
Lee, YeunkumLee, Ji SooLee, Kea JooTurner, R. ScottHoe, Hyang-SookPak, Daniel T. S.
Issue Date
May-2017
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Keywords
Alzheimer' s disease; Amyloidogenic processing; Polo-like kinase 2; Synaptic plasticity; Neuronal signaling; Neurodegeneration; Hyperexcitation
Citation
NEUROPHARMACOLOGY, v.117, pp.387 - 400
Journal Title
NEUROPHARMACOLOGY
Volume
117
Start Page
387
End Page
400
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/825
DOI
10.1016/j.neuropharm.2017.02.027
ISSN
0028-3908
Abstract
Alzheimer's disease (AD) is a neurodegenerative disorder with cognitive deficits. Amyloidogenic processing of amyloid precursor protein (APP) produces amyloid beta (A beta), the major component of hallmark AD plaques. Synaptic activity stimulates APP cleavage, whereas APP promotes excitatory synaptic transmission, suggesting APP participates in neuronal homeostasis. However, mechanisms linking synaptic activity to APP processing are unclear. Here we show that Polo-like kinase 2 (Plk2), an activity-inducible regulator of homeostatic plasticity, directly binds and phosphorylates threonine-668 and serine-675 of APP in vitro and associates with APP in vivo. Plk2 accelerates APP amyloidogenic cleavage by P-secretase at synapses and is required for neuronal overactivity-stimulated A beta secretion. These findings implicate Plk2 as a novel mediator of activity-dependent APP amyloidogenic processing. (C) 2017 Elsevier Ltd. All rights reserved.
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연구본부 (신경회로 연구그룹)
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