Journal
FEBS LETTERS
Volume 584, Issue 22, Pages 4559-4564Publisher
WILEY
DOI: 10.1016/j.febslet.2010.10.044
Keywords
Nuclear organization; Cajal Body; Coilin; Paraspeckle Protein 1; Paraspeckle
Funding
- Research Promotion Foundation of Cyprus [YGEIA/0506/05]
- MRC [G0301131, G0801738] Funding Source: UKRI
- Medical Research Council [G0801738, G0301131] Funding Source: researchfish
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hCINAP is an atypical nucleoplasmic enzyme, combining structural features of adenylate kinases and ATPases, which exhibits dual enzymatic activity. It interacts with the Cajal Body marker coilin and its level of expression and enzymatic activity influence Cajal Body numbers. Here we show that upon specific transcriptional inhibition of RNA pol.II, hCINAP segregates in perinuclear caps identified as Dark Nucleolar Caps (DNCs). These are distinct from perinucleolar caps where coilin and fibrillarin (both Cajal Body components) accumulate. In DNCs, hCINAP co-localizes with Paraspeckle Protein (PSP1) and also co-segregates with PSP1, and not coilin, in nuclear and nucleolar foci upon UV irradiation. Structured summary: MINT-8048545: hCINAP (uniprotkb:Q9Y3D8) and PSP1 (uniprotkb:Q8WXF1) colocalize (MI:0403) by fluorescence microscopy (MI: 0416) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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