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• W2116320149 endingPage "270" @default.
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• W2116320149 abstract "The cyclin-dependent kinase (CDK)-activating kinase (CAK) is involved in cell cycle control, transcription, and DNA repair (E. A. Nigg, Curr. Opin. Cell. Biol. 8:312-317, 1996). However, the mechanisms of how CAK is integrated into these signaling pathways remain unknown. We previously demonstrated that abrogation of MAT1 (ménage à trois 1), an assembly factor and targeting subunit of CAK, induces G(1) arrest (L. Wu, P. Chen, J. J. Hwang, L. W. Barsky, K. I. Weinberg, A. Jong, and V. A. Starnes, J. Biol. Chem. 274:5564-5572, 1999). This result led us to investigate how deregulation of CAK by MAT1 abrogation affects the cell cycle G(1) exit, a process that is regulated most closely by phosphorylation of retinoblastoma tumor suppressor protein (pRb). Using mammalian cellular models that undergo G(1) arrest evoked by antisense MAT1 abrogation, we found that deregulation of CAK inhibits pRb phosphorylation and cyclin E expression, CAK phosphorylation of pRb is MAT1 dose dependent but cyclin D1/CDK4 independent, and MAT1 interacts with pRb. These results suggest that CAK is involved in the regulation of cell cycle G(1) exit while MAT1-modulated CAK formation and CAK phosphorylation of pRb may determine the cell cycle specificity of CAK in G(1) progression." @default.
• W2116320149 created "2016-06-24" @default.
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• W2116320149 date "2001-01-01" @default.
• W2116320149 modified "2023-09-27" @default.
• W2116320149 title "MAT1-Modulated CAK Activity Regulates Cell Cycle G₁ Exit" @default.
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• W2116320149 doi "https://doi.org/10.1128/mcb.21.1.260-270.2001" @default.
• W2116320149 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/88799" @default.
• W2116320149 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11113200" @default.
• W2116320149 hasPublicationYear "2001" @default.
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