scholarly journals Roles of amyloid β precursor protein in neurotransmitter receptor localization and function

2019 ◽  
Vol 154 (5) ◽  
pp. 288-288
Author(s):  
Naoya Yamashita
Keyword(s):  
Amyloid Β ◽  
Precursor Protein ◽  
Neurotransmitter Receptor ◽  
Receptor Localization ◽  
And Function

scholarly journals Effects of Huanglian-Jie-Du-Tang and Its Modified Formula on the Modulation of Amyloid-β Precursor Protein Processing in Alzheimer's Disease Models

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e92954 ◽  
Author(s):  
Siva Sundara Kumar Durairajan ◽  
Ying-Yu Huang ◽  
Pui-Yee Yuen ◽  
Lei-Lei Chen ◽  
Ka-Yan Kwok ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Protein Processing ◽  
Precursor Protein ◽  
Disease Models ◽  
Modified Formula

scholarly journals Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein

2016 ◽  
Vol 27 (20) ◽  
pp. 3031-3039 ◽  
Author(s):  
Michael W. Woellhaf ◽  
Frederik Sommer ◽  
Michael Schroda ◽  
Johannes M. Herrmann
Keyword(s):  
Precursor Protein ◽  
Ribosomal Biogenesis ◽  
Proteomic Profiling ◽  
Mitochondrial Translation ◽  
Bacterial Ribosome ◽  
Mitochondrial Ribosome ◽  
Translation Apparatus ◽  
The Matrix ◽  
Processing Peptidase ◽  
And Function

Whereas the structure and function of cytosolic ribosomes are well characterized, we only have a limited understanding of the mitochondrial translation apparatus. Using SILAC-based proteomic profiling, we identified 13 proteins that cofractionated with the mitochondrial ribosome, most of which play a role in translation or ribosomal biogenesis. One of these proteins is a homologue of the bacterial ribosome-silencing factor (Rsf). This protein is generated from the composite precursor protein Atp25 upon internal cleavage by the matrix processing peptidase MPP, and in this respect, it differs from all other characterized mitochondrial proteins of baker’s yeast. We observed that cytosolic expression of Rsf, but not of noncleaved Atp25 protein, is toxic. Our results suggest that eukaryotic cells face the challenge of avoiding negative interference from the biogenesis of their two distinct translation machineries.

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