Dynamic interaction of p220(NPAT) and CBP/p300 promotes S-phase entry.
Cajal bodies contain cyclin E/cdk2 and the substrate p220(NPAT) to regulate the transcription of histones, which is essential for cell proliferation, however, recent mouse knockout studies indicate that cyclin E and cdk2 are dispensable for these events. Because the CBP/p300 histone acetyltransferase are also known to be involved in cell ... proliferation, we examined the molecular and functional interactions of p220(NPAT) with the CBP/p300 at the G1/S boundary as cell cycle regulators. The subnuclear localization of p220(NPAT) and CBP/p300 proteins showed that their foci partially overlapped in a cell cycle dependent manner. Overexpression of p220(NPAT) and CBP/p300 cooperatively enhanced G1/S transition and DNA synthesis even without cdk2 phosphorylation site. Finally, molecular alignment analysis indicated that p220(NPAT) contains several potential substrate sites for CBP/p300. Overall, our findings demonstrate that p220(NPAT) and CBP/p300 form a transient complex at the G1/S boundary to play cooperative roles to promote the S-phase entry.
Mesh Terms:
Amino Acid Sequence, Cell Cycle Proteins, Cell Line, Tumor, Cell Proliferation, Coiled Bodies, DNA, Humans, Molecular Sequence Data, Nuclear Proteins, Osteosarcoma, S Phase, Trans-Activators
Amino Acid Sequence, Cell Cycle Proteins, Cell Line, Tumor, Cell Proliferation, Coiled Bodies, DNA, Humans, Molecular Sequence Data, Nuclear Proteins, Osteosarcoma, S Phase, Trans-Activators
Biochem. Biophys. Res. Commun.
Date: Dec. 24, 2004
PubMed ID: 15555599
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