| Literature DB >> 22122073 |
P St George-Hyslop1,2, P E Fraser1,3.
Abstract
The presenilin complex is composed of four core proteins (presenilin 1 or presenilin 2, APH1, nicastrin, and PEN2). Several endogenous proteins have been reported to selectively modulate the function of the presenilin complexes; these include transmembrane trafficking protein, 21-KD (TMP21), CD147 antigen (basigin), the γ-secretase-activating protein (gSAP), and the orphan G-protein-coupled receptor 3. Because the structure and assembly of these complexes underlies their activity, this review will discuss current work on the assembly of the complex and on presenilin-interacting proteins that regulate secretase activity.Entities:
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Year: 2011 PMID: 22122073 DOI: 10.1111/j.1471-4159.2011.07505.x
Source DB: PubMed Journal: J Neurochem ISSN: 0022-3042 Impact factor: 5.546