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Assembly of the presenilin γ‐/ε‐secretase complex
Author(s) -
St GeorgeHyslop P.,
Fraser P. E.
Publication year - 2012
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2011.07505.x
Subject(s) - presenilin , nicastrin , transmembrane protein , basigin , microbiology and biotechnology , biology , chemistry , biochemistry , receptor , alzheimer's disease , medicine , disease , matrix metalloproteinase , pathology
J. Neurochem. (2012) 120 (Suppl. 1), 84–88. 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.