Cell Biology

Capturing Immature Components

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Science  16 Mar 2007:
Vol. 315, Issue 5818, pp. 1467
DOI: 10.1126/science.315.5818.1467d

The γ-secretase complex catalyzes proteolytic cleavage of a variety of membrane proteins, including the amyloid precursor protein that is implicated in Alzheimer's disease. The complex contains several components, including presenilin, anterior pharynx defective-1 (APH-1), and nicastrin. Spasic et al. have examined the intracellular assembly path of this complex and have found that a protein involved in recycling within the early secretory pathway, Rer1p, interacts with immature nicastrin either in the Golgi or in the endoplasmic reticulum (ER): the entry portal to the secretory pathway. It seems that Rer1p effectively binds to a site within the transmembrane domain of nicastrin that can also interact with APH-1 in the mature γ-secretase complex. Rer1p-binding competes with the assembly of APH-1 and nicastrin and also returns to the ER any immature nicastrin that has escaped into the Golgi. — SMH

J. Cell Biol. 176, 629 (2007).

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