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O4‐03–02: Gamma‐secretase localization and function at synapses
Author(s) -
Restituito Sophie,
Burette Susan,
Phend Kristen,
Weinberg Richard,
Ziff Edward B.
Publication year - 2008
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2008.05.519
Subject(s) - presenilin , ampa receptor , nicastrin , synapse , microbiology and biotechnology , gamma secretase , synaptic plasticity , amyloid precursor protein secretase , biology , chemistry , amyloid precursor protein , neuroscience , biochemistry , nmda receptor , receptor , alzheimer's disease , medicine , disease , pathology
mature APP and the secreted form of APP were significantly decreased in cells overexpressing Rer1. In contrast, surface labeling by fluorescently labeled lectin was not significantly affected, indicating that the effects of Rer1 on the maturation of nicastrin and APP are not due to nonspecific effects on surface glycoproteins. Conclusions: These results indicate that Rer1 is the limiting cellular factor for the ER retrieval of gamma-secretase complex and that it also plays a role in the regulation of APP trafficking.