Structure-activity relationship of presenilin in γ-secretase-mediated intramembrane cleavage
| Autor: | Tetsuo Cai, Taisuke Tomita |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Intramembrane protease Proteolysis Protein subunit medicine.medical_treatment Nicastrin Presenilin Structure-Activity Relationship 03 medical and health sciences 0302 clinical medicine medicine Humans Protease medicine.diagnostic_test biology Presenilins Membrane Proteins Cell Biology medicine.disease Cell biology 030104 developmental biology Membrane protein biology.protein Amyloid Precursor Protein Secretases Alzheimer's disease 030217 neurology & neurosurgery Developmental Biology |
| Zdroj: | Seminars in Cell & Developmental Biology. 105:102-109 |
| ISSN: | 1084-9521 |
| DOI: | 10.1016/j.semcdb.2020.02.006 |
| Popis: | Genetic research on familial cases of Alzheimer disease have identified presenilin (PS) as an important membrane protein in the pathomechanism of this disease. PS is the catalytic subunit of γ-secretase, which is responsible for the generation of amyloid-β peptide deposited in the brains of Alzheimer disease patients. γ-Secretase is an atypical protease composed of four membrane proteins (i.e., presenilin, nicastrin, anterior pharynx defective-1 (Aph-1), and presenilin enhancer-2 (Pen-2)) and mediates intramembrane proteolysis. Numerous investigations have been conducted toward understanding the structural features of γ-secretase components as well as the cleavage mechanism of γ-secretase. In this review, we summarize our current understanding of the structure and activity relationship of the γ-secretase complex. |
| Databáze: | OpenAIRE |
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