期刊
JOURNAL OF CELL SCIENCE
卷 116, 期 2, 页码 303-312出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.00211
关键词
RNA processing; nuclear bodies; phosphorylation; SMN; snRNA; snoRNA
类别
资金
- NICHD NIH HHS [HD07518] Funding Source: Medline
- NIGMS NIH HHS [GM08613, GM53034, R01 GM053034] Funding Source: Medline
- NINDS NIH HHS [NS41617] Funding Source: Medline
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.
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