|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
First published online 27 November 2002
doi: 10.1242/jcs.00211
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Research Article |

Department of Genetics, Center for Human Genetics and Program in Cell
Biology, Case Western Reserve University and University Hospitals of
Cleveland, Cleveland, OH 44106-4955, USA
Present address: Department of Biochemistry, University of Mississippi Medical
Center, Jackson, MS 39216-4505, USA
* Author for correspondence (e-mail: gxm26{at}po.cwru.edu)
Accepted 6 October 2002
Cajal bodies (CBs) are nuclear suborganelles implicated in the post-transcriptional maturation of small nuclear and small nucleolar RNAs. The number of CBs displayed by various cell lines and tissues varies, and factors that control CB numbers within a given cell have yet to be described. In this report, we show that specific regions within the C-terminus of coilin, the CB marker protein, are responsible for regulating the number of nuclear foci. Despite the fact that the coilin N-terminal domain is responsible for its self-oligomerization activity, truncation or mutation of predicted sites of phosphorylation in the conserved C-terminal region leads to a striking alteration in the number of nuclear bodies. Similarly, coilin constructs from various species display differential propensities to form nuclear foci when expressed in heterologous backgrounds. We mapped the domain responsible for this variability to the coilin C-terminus utilizing chimeric proteins. Furthermore, the activities responsible for regulating coilin self-association must reside in the nucleus, as constructs lacking critical nuclear localization sequences fail to form foci in the cytoplasm. Factors controlling the putative signal transduction cascade that phosphorylates coilin are also discussed. The results point to a model whereby phosphorylation of the coilin C-terminus regulates the availability of the N-terminal self-interaction domain.
Key words: RNA processing, Nuclear bodies, Phosphorylation, SMN, snRNA, snoRNA
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati
Twitter What's this?
This article has been cited by other articles:
![]() |
A.-F. Bruns, J. van Bergeijk, C. Lorbeer, A. Nolle, J. Jungnickel, C. Grothe, and P. Claus Fibroblast growth factor-2 regulates the stability of nuclear bodies PNAS, August 4, 2009; 106(31): 12747 - 12752. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Gangwani, R. A. Flavell, and R. J. Davis ZPR1 Is Essential for Survival and Is Required for Localization of the Survival Motor Neurons (SMN) Protein to Cajal Bodies Mol. Cell. Biol., April 1, 2005; 25(7): 2744 - 2756. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Dundr, M. D. Hebert, T. S. Karpova, D. Stanek, H. Xu, K. B. Shpargel, U. T. Meier, K. M. Neugebauer, A. G. Matera, and T. Misteli In vivo kinetics of Cajal body components J. Cell Biol., March 15, 2004; 164(6): 831 - 842. [Abstract] [Full Text] [PDF] |
||||
![]() |
X. Ye, Y. Wei, G. Nalepa, and J. W. Harper The Cyclin E/Cdk2 Substrate p220NPAT Is Required for S-Phase Entry, Histone Gene Expression, and Cajal Body Maintenance in Human Somatic Cells Mol. Cell. Biol., December 1, 2003; 23(23): 8586 - 8600. [Abstract] [Full Text] [PDF] |
||||