Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control
Article first published online: 14 DEC 2001
Copyright © 2002 Wiley-Liss, Inc.
Journal of Cellular Physiology
Volume 190, Issue 2, pages 160–169, February 2002
How to Cite
Oelgeschläger, T. (2002), Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control. J. Cell. Physiol., 190: 160–169. doi: 10.1002/jcp.10058
- Issue published online: 4 JAN 2002
- Article first published online: 14 DEC 2001
- Manuscript Accepted: 11 SEP 2001
- Manuscript Received: 29 AUG 2001
The carboxyl-terminal domain (CTD) of the largest subunit of mammalian RNA polymerase II (RNAP II) consists of 52 repeats of a consensus heptapeptide and is subject to phosphorylation and dephosphorylation events during each round of transcription. RNAP II activity is regulated during the cell cycle and cell cycle-dependend changes in RNAP II activity correlate well with CTD phosphorylation. In addition, global changes in the CTD phosphorylation status are observed in response to mitogenic or cytostatic signals such as growth factors, mitogens and DNA-damaging agents. Several CTD kinases are members of the cyclin-dependent kinase (CDK) superfamily and associate with transcription initiation complexes. Other CTD kinases implicated in cell cycle regulation include the mitogen-activated protein kinases ERK-1/2 and the c-Abl tyrosine kinase. These observations suggest that reversible RNAP II CTD phosphorylation may play a key role in linking cell cycle regulatory events to coordinated changes in transcription. J. Cell. Physiol. 190: 160–169, 2002. © 2002 Wiley-Liss, Inc.