PIM-induced phosphorylation of Notch3 promotes breast cancer tumorigenicity in a CSL-independent fashion

• Published in: The Journal of biological chemistry Vol. 296; p. 100593
• Main Authors: Landor, Sebastian K.J., Santio, Niina M., Eccleshall, William B., Paramonov, Valeriy M., Gagliani, Ellen K., Hall, Daniel, Jin, Shao-Bo, Dahlström, Käthe M., Salminen, Tiina A., Rivero-Müller, Adolfo, Lendahl, Urban, Kovall, Rhett A., Koskinen, Päivi J., Sahlgren, Cecilia
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.01.2021; American Society for Biochemistry and Molecular Biology
• Subjects: 60 APPLIED LIFE SCIENCES; Active Transport, Cell Nucleus; Animals; breast cancer; Breast Neoplasms - pathology; Carcinogenesis; Cell Line, Tumor; Cell Nucleus - metabolism; Humans; Immunoglobulin J Recombination Signal Sequence-Binding Protein - metabolism; Medicin och hälsovetenskap; Mice; Models, Molecular; Muscle Proteins - metabolism; Notch proteins; Phosphorylation; PIM kinases; Protein Domains; protein–protein interaction; Proto-Oncogene Proteins c-pim-1 - metabolism; Receptor, Notch3 - chemistry; Receptor, Notch3 - metabolism; transcription regulation; tumor cell biology; transcription regulation; PIM kinases; PAS; DLL; DMSO; N1ICD; N3ICD; protein–protein interaction; RBPJ; SA; PDB; GFP; CHX; SE; DHPCC-9; HEY1; HES1; N3RAM; phosphorylation; CSL; RFP; KI; Notch proteins; breast cancer; ICD; ER; CAM; NICD; ITC; tumor cell biology; RAM

Dysregulation of the developmentally important Notch signaling pathway is implicated in several types of cancer, including breast cancer. However, the specific roles and regulation of the four different Notch receptors have remained elusive. We have previously reported that the oncogenic PIM kinases...