The nuclear ATPase/adenylate kinase hCINAP is recruited to perinucleolar caps generated upon RNA pol.II inhibition

Anna Malekkou, Carsten W. Lederer, Angus I. Lamond, Niovi Santama

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)4559-4564
    Number of pages6
    JournalFEBS Letters
    Volume584
    Issue number22
    DOIs
    Publication statusPublished - 19 Nov 2010

    Keywords

    • Nuclear organization
    • Cajal Body
    • Coilin
    • Paraspeckle Protein 1
    • Paraspeckle
    • NUCLEOLAR CAPS
    • COILED BODIES
    • CAJAL BODIES
    • BODY
    • DIFFERENTIATION
    • REORGANIZATION
    • PARASPECKLES
    • ASSOCIATION

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