scholarly journals The Impact of a Novel Apolipoprotein E and Amyloid-β Protein Precursor-Interacting Protein on the Production of Amyloid-β

2011 ◽  
Vol 26 (2) ◽  
pp. 239-253 ◽  
Author(s):  
Paul C.R. Hopkins ◽  
Ricardo Sáinz-Fuertes ◽  
Simon Lovestone
Keyword(s):  
Apolipoprotein E ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Interacting Protein ◽  
Protein Precursor ◽  
Β Protein ◽  
The Impact

scholarly journals Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1

2017 ◽  
Vol 28 (26) ◽  
pp. 3857-3869 ◽  
Author(s):  
Kyoko Chiba ◽  
Ko-yi Chien ◽  
Yuriko Sobu ◽  
Saori Hata ◽  
Shun Kato ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Amyloid Β ◽  
Tetratricopeptide Repeat ◽  
Amyloid Β Protein ◽  
The Novel ◽  
Anterograde Transport ◽  
Interacting Protein ◽  
Protein Precursor ◽  
Kinesin Light Chain ◽  
Β Protein

In neurons, amyloid β-protein precursor (APP) is transported by binding to kinesin-1, mediated by JNK-interacting protein 1b (JIP1b), which generates the enhanced fast velocity (EFV) and efficient high frequency (EHF) of APP anterograde transport. Previously, we showed that EFV requires conventional interaction between the JIP1b C-terminal region and the kinesin light chain 1 (KLC1) tetratricopeptide repeat, whereas EHF requires a novel interaction between the central region of JIP1b and the coiled-coil domain of KLC1. We found that phosphorylatable Thr466 of KLC1 regulates the conventional interaction with JIP1b. Substitution of Glu for Thr466 abolished this interaction and EFV, but did not impair the novel interaction responsible for EHF. Phosphorylation of KLC1 at Thr466 increased in aged brains, and JIP1 binding to kinesin-1 decreased, suggesting that APP transport is impaired by aging. We conclude that phosphorylation of KLC1 at Thr466 regulates the velocity of transport of APP by kinesin-1 by modulating its interaction with JIP1b.

scholarly journals Amyloid β Protein Precursor Is Phosphorylated by JNK-1 Independent of, yet Facilitated by, JNK-Interacting Protein (JIP)-1

2003 ◽  
Vol 278 (43) ◽  
pp. 42058-42063 ◽  
Author(s):  
Meir H. Scheinfeld ◽  
Enrico Ghersi ◽  
Peter Davies ◽  
Luciano D'Adamio
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Interacting Protein ◽  
Protein Precursor ◽  
Β Protein

scholarly journals Amyloid-β Oligomers Induce Only Mild Changes to Inhibitory Bouton Dynamics

2021 ◽  
Vol 5 (1) ◽  
pp. 153-160 ◽  
Author(s):  
Marvin Ruiter ◽  
Christine Lützkendorf ◽  
Jian Liang ◽  
Corette J. Wierenga
Keyword(s):  
Hippocampal Slices ◽  
Inhibitory Neuron ◽  
Amyloid Β ◽  
Inhibitory Neurons ◽  
Inhibitory Synapses ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Β Protein ◽  
Plaque Load ◽  
Early Alzheimer’S Disease

The amyloid-β protein precursor is highly expressed in a subset of inhibitory neuron in the hippocampus, and inhibitory neurons have been suggested to play an important role in early Alzheimer’s disease plaque load. Here we investigated bouton dynamics in axons of hippocampal interneurons in two independent amyloidosis models. Short-term (24 h) amyloid-β (Aβ)-oligomer application to organotypic hippocampal slices slightly increased inhibitory bouton dynamics, but bouton density and dynamics were unchanged in hippocampus slices of young-adult AppNL - F - G-mice, in which Aβ levels are chronically elevated. These results indicate that loss or defective adaptation of inhibitory synapses are not a major contribution to Aβ-induced hyperexcitability.

The upstream stimulatory factor functionally interacts with the Alzheimer amyloid β-protein precursor gene

1995 ◽  
Vol 4 (9) ◽  
pp. 1527-1533 ◽  
Author(s):  
Dora M. Kovacs ◽  
Wilma Wasco ◽  
Johanna Witherby ◽  
Kevin M. Felsenstein ◽  
Franck Brunei ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Upstream Stimulatory Factor ◽  
Protein Precursor ◽  
Β Protein ◽  
Stimulatory Factor
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