期刊
CANCERS
卷 14, 期 5, 页码 -出版社
MDPI
DOI: 10.3390/cancers14051345
关键词
Casein Kinase 1; CK1; RITA; microtubule dynamics; cell cycle progression; microtubule transport; microtubule-associated proteins; MAPs; mitotic spindle; tumorigenesis
类别
资金
- International Graduate School in Molecular Medicine at Ulm University (IGradU)
- German Research Foundation (DFG) [GSC 270]
- DFG [GRK2254/C4, SFB1074/A3, SFB1506/A5, OS 287/4-1, KN356/9-1]
- German Cancer Aid (Deutsche Krebshilfe) [70114289]
- Else Kroener-Fresenius-Stiftung [2017_A142]
Protein kinases of the Casein Kinase 1 family are essential for the regulation of various cellular processes, including microtubule dynamics. They directly modulate microtubule dynamics by phosphorylating tubulin isoforms and microtubule-associated proteins, which can affect microtubule stability and genomic stability. Therefore, targeting Casein Kinase 1 functions may be a potential therapeutic strategy for cancer treatment.
Protein kinases of the Casein Kinase 1 family play a vital role in the regulation of numerous cellular processes. Apart from functions associated with regulation of proliferation, differentiation, or apoptosis, localization of several Casein Kinase 1 isoforms to the centrosome and microtubule asters also implicates regulatory functions in microtubule dynamic processes. Being localized to the spindle apparatus during mitosis Casein Kinase 1 directly modulates microtubule dynamics by phosphorylation of tubulin isoforms. Additionally, site-specific phosphorylation of microtubule-associated proteins can be related to the maintenance of genomic stability but also microtubule stabilization/destabilization, e.g., by hyper-phosphorylation of microtubule-associated protein 1A and RITA. Consequently, approaches interfering with Casein Kinase 1-mediated microtubule-specific functions might be exploited as therapeutic strategies for the treatment of cancer. Currently pursued strategies include the development of Casein Kinase 1 isoform-specific small molecule inhibitors and therapeutically useful peptides specifically inhibiting kinase-substrate interactions.
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