Journal
CELL CYCLE
Volume 11, Issue 18, Pages 3389-3394Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/cc.21404
Keywords
DYRK1A; DYRK1B; DYRK2; HIPK2; MBK-2; Yak1; phosphodegron; ubiquitin cyclin D1; p27(Kip1)
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Funding
- Deutsche Forschungsgemeinschaft [BE 1967/2-1]
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Dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs) constitute an evolutionarily conserved family of protein kinases with key roles in the control of cell proliferation and differentiation. Members of the DYRK family phosphorylate many substrates, including critical regulators of the cell cycle. A recent report revealed that human DYRK2 acts as a negative regulator of G(1)/S transition by phosphorylating c-Jun and c-Myc, thereby inducing ubiquitination-mediated degradation. Other DYRKs also function as cell cycle regulators by modulating the turnover of their target proteins. DYRK1B can induce reversible cell arrest in a quiescent G(0) state by targeting cyclin D1 for proteasomal degradation and stabilizing p27(Kip1). The DYRK2 ortholog of C. elegans, MBK-2, triggers the proteasomal destruction of oocyte proteins after meiosis to allow the mitotic divisions in embryo development. This review summarizes the accumulating results that provide evidence for a general role of DYRKs in the regulation of protein stability.
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