P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner

Archa H. Fox, Charles S. Bond, Angus I. Lamond (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    150 Citations (Scopus)

    Abstract

    P54nrb is a protein implicated in multiple nuclear processes whose specific functions may correlate with its presence at different nuclear locations. Here we characterize paraspeckles, a subnuclear domain containing p54nrb and other RNA-binding proteins including PSP1, a protein with sequence similarity to p54nrb that acts as a marker for paraspeckles. We show that PSP1 interacts in vivo with a subset of the total cellular pool of p54nrb. We map the domain within PSP1 that is mediating this interaction and show it is required for the correct localization of PSP1 to paraspeckles. This interaction is necessary but not sufficient for paraspeckle targeting by PSP1, which also requires an RRM capable of RNA binding. Blocking the reinitiation of RNA Pol II transcription at the end of mitosis with DRB prevents paraspeckle formation, which recommences after removal of DRB, indicating that paraspeckle formation is dependent on RNA Polymerase II transcription. Thus paraspeckles are the sites where a subset of the total cellular pool of p54nrb is targeted in a RNA Polymerase II-dependent manner.

    Original languageEnglish
    Pages (from-to)5304-5315
    Number of pages12
    JournalMolecular Biology of the Cell
    Volume16
    Issue number11
    DOIs
    Publication statusPublished - 1 Nov 2005

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