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Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.

التفاصيل البيبلوغرافية
العنوان: Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.
المؤلفون: Jung-Soon Mo, Ji-Hye Yoon, Ji-Ae Hong, Mi-Yeon Kim, Eun-Jung Ann, Ji-Seon Ahn, Su-Man Kim, Hyeong-Jin Baek, Florian Lang, Eui-Ju Choi, Hee-Sae Park
المصدر: PLoS ONE, Vol 7, Iss 5, p e37111 (2012)
بيانات النشر: Public Library of Science (PLoS), 2012.
سنة النشر: 2012
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: The gamma-secretase complex is involved in the intramembranous proteolysis of a variety of substrates, including the amyloid precursor protein and the Notch receptor. Nicastrin (NCT) is an essential component of the gamma-secretase complex and functions as a receptor for gamma-secretase substrates. In this study, we determined that serum- and glucocorticoid-induced protein kinase 1 (SGK1) markedly reduced the protein stability of NCT. The SGK1 kinase activity was decisive for NCT degradation and endogenous SGK1 inhibited gamma-secretase activity. SGK1 downregulates NCT protein levels via proteasomal and lysosomal pathways. Furthermore, SGK1 directly bound to and phosphorylated NCT on Ser437, thereby promoting protein degradation. Collectively, our findings indicate that SGK1 is a gamma-secretase regulator presumably effective through phosphorylation and degradation of NCT.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
44069278
Relation: http://europepmc.org/articles/PMC3349648?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0037111
URL الوصول: https://doaj.org/article/f0e44069278641f68803c0c9b434e454
رقم الأكسشن: edsdoj.f0e44069278641f68803c0c9b434e454
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
44069278
DOI:10.1371/journal.pone.0037111