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Fig. 3 | Cell & Bioscience

Fig. 3

From: Cholesterol-dependent amyloid β production: space for multifarious interactions between amyloid precursor protein, secretases, and cholesterol

Fig. 3

Dimerization of C99 and implications for γ-secretase-mediated processing. A Three glycine zippers are located in the TM segment and j.m. region of C99 (G25-x-x-x-G29; G29-x-x-x-G33; G33-x-x-x-G37/G38). Close positioning of the two monomers is required for dimerization. B Shifts and rotations of the TM helices caused by distinct Gly zipper interactions affect (1) the start cleavage site for γ-secretase because different amino acid sequences are exposed to the catalytic site, and (2) the stop of cleavage due to steric hindrance by tightly bound parts of the monomers. If the secretase cannot continue cleavage, longer and more dangerous amyloid β forms (amyloid β42) will be released. Adjusted according to [205, 237, 253, 267,268,269,270]

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Cell & Bioscience

ISSN: 2045-3701

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