PEN-2 enhances gamma-cleavage after presenilin heterodimer formation
نویسندگان
چکیده
منابع مشابه
Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrin.
Mutations in presenilin proteins (PS1 and PS2) lead to early-onset Alzheimer's disease. PS proteins are endoproteolytically cleaved into two main fragments: the NTF (PS N-terminal fragment) and the CTF (PS C-terminal fragment). The two fragments are believed to constitute the core catalytic enzyme activity called gamma-secretase, which is responsible for cleaving beta-amyloid precursor protein ...
متن کاملGamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2.
gamma-Secretase catalyzes the intramembrane proteolysis of Notch, beta-amyloid precursor protein, and other substrates as part of a new signaling paradigm and as a key step in the pathogenesis of Alzheimer's disease. This unusual protease has eluded identification, though evidence suggests that the presenilin heterodimer comprises the catalytic site and that a highly glycosylated form of nicast...
متن کاملPEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1.
Presenilin (PS, PS1/PS2) complexes are known to be responsible for the intramembranous gamma-secretase cleavage of the beta-amyloid precursor protein and signaling receptor Notch. PS holoprotein undergoes endoproteolysis by an unknown enzymatic activity to generate NH(2)- and COOH-terminal fragments, a process that is required for the formation of the active and stable PS/-gamma-secretase compl...
متن کاملAph-1, Pen-2, and Nicastrin with Presenilin Generate an Active γ-Secretase Complex
mechanism needs further scrutiny, -Secretase may -Secretase cleaves the Amyloid Precursor Protein therefore indeed be considered an aspartyl protease (APP) in its transmembrane domain, releasing the am(Wolfe et al., 1999). PS are synthesized as precursor yloid peptide A . A is the main constituent of the proteins that must become incorporated into a larger amyloid plaques in the brains of patie...
متن کاملHsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation.
ErbB-2/HER2 is an oncogenic tyrosine kinase that regulates a signalling network by forming ligand-induced heterodimers with several growth factor receptors of the ErbB family. Hsp90 and co-chaperones regulate degradation of ErbB-2 but not other ErbB members. Here, we report that the role of Hsp90 in modulating the ErbB network extends beyond regulation of protein stability. The capacity of ErbB...
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ژورنال
عنوان ژورنال: Journal of Neurochemistry
سال: 2004
ISSN: 0022-3042,1471-4159
DOI: 10.1111/j.1471-4159.2004.02597.x