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1-4 of 4
Keywords: CK1
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Journal Articles
Alaina H. Willet, Maya G. Igarashi, Jun-Song Chen, Rahul Bhattacharjee, Liping Ren, Sierra N. Cullati, Zachary C. Elmore, Rachel H. Roberts-Galbraith, Alyssa E. Johnson, Janel R. Beckley, Kathleen L. Gould
Journal:
Journal of Cell Science
J Cell Sci (2021) 134 (16): jcs258645.
Published: 17 August 2021
... phosphoregulated. We found that Imp2 is endogenously phosphorylated on 28 sites within its IDR, with the bulk of phosphorylation being constitutive. In vitro , the casein kinase 1 (CK1) isoforms Hhp1 and Hhp2 can phosphorylate 17 sites, and Cdk1 (also known as Cdc2) can phosphorylate the remaining 11 sites...
Includes: Supplementary data
Journal Articles
HIF-2α phosphorylation by CK1δ promotes erythropoietin secretion in liver cancer cells under hypoxia
Evanthia Pangou, Christina Befani, Ilias Mylonis, Martina Samiotaki, George Panayotou, George Simos, Panagiotis Liakos
Journal:
Journal of Cell Science
J Cell Sci (2016) 129 (22): 4213–4226.
Published: 15 November 2016
... ). The CK1 family: contribution to cellular stress response and its role in carcinogenesis . Front. Oncol. 4 , 96 . 10.3389/fonc.2014.00096 Koh , M. Y. , Darnay , B. G. and Powis , G. ( 2008 ). Hypoxia-associated factor, a novel E3-ubiquitin ligase, binds and ubiquitinates hypoxia...
Includes: Supplementary data
Journal Articles
Alkmini Kalousi, Ilias Mylonis, Anastasia S. Politou, Georgia Chachami, Efrosyni Paraskeva, George Simos
Journal:
Journal of Cell Science
J Cell Sci (2010) 123 (17): 2976–2986.
Published: 1 September 2010
...)-mediated silencing of CK1δ under hypoxic conditions. Conversely, overexpression of CK1δ or phosphomimetic mutation of Ser247 to aspartate inhibited HIF-1α activity without affecting its stability or nuclear accumulation. Immunoprecipitation and in vitro binding experiments suggest that CK1-dependent...
Includes: Supplementary data
Journal Articles
Journal:
Journal of Cell Science
J Cell Sci (2002) 115 (1): 217–226.
Published: 1 January 2002
... sequence. The phosphorylation of these residues facilitates the ubiquitination and internalization of the permease. Following endocytosis, the permease is targeted to the lysosome/vacuole for proteolysis. We have shown that in casein kinase 1 (CK1)-deficient cells, the permease is poorly phosphorylated...