BMB Rep. 2015; 48(8): 431-437  
Phosphorylation-dependent regulation of Notch1 signaling: the fulcrum of Notch1 signaling
Hye-Jin Lee, Mi-Yeon Kim & Hee-Sae Park*
Hormone Research Center, School of Biological Sciences and Technology, Chonnam National University, Gwangju 61186, Korea
Correspondence to: Tel: +82-62-530-0021; Fax: +82-62-530-2199; E-mail: proteome@jnu.ac.kr
Received: June 2, 2015; Published online: August 31, 2015.
© Korean Society for Biochemistry and Molecular Biology. All rights reserved.

Abstract
Notch signaling plays a pivotal role in cell fate determination, cellular development, cellular self-renewal, tumor progression, and has been linked to developmental disorders and carcinogenesis. Notch1 is activated through interactions with the ligands of neighboring cells, and acts as a transcriptional activator in the nucleus. The Notch1 intracellular domain (Notch1-IC) regulates the expression of target genes related to tumor development and progression. The Notch1 protein undergoes modification after translation by posttranslational modification enzymes. Phosphorylation modification is critical for enzymatic activation, complex formation, degradation, and subcellular localization. According to the nuclear cycle, Notch1-IC is degraded by E3 ligase, FBW7 in the nucleus via phosphorylation-dependent degradation. Here, we summarize the Notch signaling pathway, and resolve to understand the role of phosphorylation in the regulation of Notch signaling as well as to understand its relation to cancer.
Keywords: Cancer, Degradation, Kinase, Notch1, Phosphorylation


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