Paraspeckles: a novel nuclear domain

Archa H. Fox, Yun Wah Lam, Anthony K. L. Leung, Carol E. Lyon, Jens Andersen, Matthias Mann, Angus I. Lamond

    Research output: Contribution to journalArticle

    306 Citations (Scopus)

    Abstract

    Background: The cell nucleus contains distinct classes of subnuclear bodies, including nucleoli, splicing speckles, Cajal bodies, gems, and PML bodies. Many nuclear proteins are known to interact dynamically with one or other of these bodies, and disruption of the specific organization of nuclear proteins can result in defects in cell functions and may cause molecular disease. Results: A proteomic study of purified human nucleoli has identified novel proteins, including Paraspeckle Protein 1 (PSP1) (see accompanying article, this issue of Current Biology). Here we show that PSP1 accumulates in a new nucleoplasmic compartment, termed paraspeckles, that also contains at least two other protein components: PSP2 and p54/nrb. A similar pattern of typically 10 to 20 paraspeckles was detected in all human cell types analyzed, including primary and transformed cells. Paraspeckles correspond to discrete bodies in the interchromatin nucleoplasmic space that are often located adjacent to splicing speckles. A stable cell line expressing YFP-PSP1 has been established and used to demonstrate that PSP1 interacts dynamically with nucleoli and paraspeckles in living cells. The three paraspeckle proteins relocalize quantitatively to unique cap structures at the nucleolar periphery when transcription is inhibited. Conclusions: We have identified a novel nuclear compartment, termed paraspeckles, found in both primary and transformed human cells. Paraspeckles contain at least three RNA binding proteins that all interact dynamically with the nucleolus in a transcription-dependent fashion.
    Original languageEnglish
    Pages (from-to)13-24
    Number of pages12
    JournalCurrent Biology
    Volume12
    Issue number1
    DOIs
    Publication statusPublished - Jan 2002

    Fingerprint

    cell nucleolus
    Cells
    Proteins
    proteins
    nuclear proteins
    Transcription
    Speckle
    Nuclear Proteins
    cells
    transcription (genetics)
    Gems
    RNA-binding proteins
    RNA-Binding Proteins
    cell nucleus
    Cell Nucleus
    Proteomics
    proteomics
    cell lines
    Cell Line
    Biological Sciences

    Cite this

    Fox, A. H., Lam, Y. W., Leung, A. K. L., Lyon, C. E., Andersen, J., Mann, M., & Lamond, A. I. (2002). Paraspeckles: a novel nuclear domain. Current Biology, 12(1), 13-24. https://doi.org/10.1016/S0960-9822(01)00632-7
    Fox, Archa H. ; Lam, Yun Wah ; Leung, Anthony K. L. ; Lyon, Carol E. ; Andersen, Jens ; Mann, Matthias ; Lamond, Angus I. / Paraspeckles: a novel nuclear domain. In: Current Biology. 2002 ; Vol. 12, No. 1. pp. 13-24.
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    title = "Paraspeckles: a novel nuclear domain",
    abstract = "Background: The cell nucleus contains distinct classes of subnuclear bodies, including nucleoli, splicing speckles, Cajal bodies, gems, and PML bodies. Many nuclear proteins are known to interact dynamically with one or other of these bodies, and disruption of the specific organization of nuclear proteins can result in defects in cell functions and may cause molecular disease. Results: A proteomic study of purified human nucleoli has identified novel proteins, including Paraspeckle Protein 1 (PSP1) (see accompanying article, this issue of Current Biology). Here we show that PSP1 accumulates in a new nucleoplasmic compartment, termed paraspeckles, that also contains at least two other protein components: PSP2 and p54/nrb. A similar pattern of typically 10 to 20 paraspeckles was detected in all human cell types analyzed, including primary and transformed cells. Paraspeckles correspond to discrete bodies in the interchromatin nucleoplasmic space that are often located adjacent to splicing speckles. A stable cell line expressing YFP-PSP1 has been established and used to demonstrate that PSP1 interacts dynamically with nucleoli and paraspeckles in living cells. The three paraspeckle proteins relocalize quantitatively to unique cap structures at the nucleolar periphery when transcription is inhibited. Conclusions: We have identified a novel nuclear compartment, termed paraspeckles, found in both primary and transformed human cells. Paraspeckles contain at least three RNA binding proteins that all interact dynamically with the nucleolus in a transcription-dependent fashion.",
    author = "Fox, {Archa H.} and Lam, {Yun Wah} and Leung, {Anthony K. L.} and Lyon, {Carol E.} and Jens Andersen and Matthias Mann and Lamond, {Angus I.}",
    note = "dc.publisher: Elsevier dc.description.sponsorship: A.I.L. is a Wellcome Trust Principal Research Fellow and is funded by a Wellcome Trust Programme grant. A.H.F. is funded by a Wellcome Trust International Travelling Fellowship; A.K.L.L. is funded by a Croucher studentship; Y.W.L. is funded by a Croucher postdoctoral fellowship; and C.E.L. is funded by the Wellcome Trust. We would like to thank Dr. K. Collins for the 1787htert cell line. Work in M.M.'s laboratory is funded by a Danish National Research Foundation grant to the Centre for Experimental BioInformatics. We thank Dr. B. Frenguelli and Dr. C. Connolly from Ninewells Hospital, Dundee, for the use of the LSM510.",
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    Fox, AH, Lam, YW, Leung, AKL, Lyon, CE, Andersen, J, Mann, M & Lamond, AI 2002, 'Paraspeckles: a novel nuclear domain', Current Biology, vol. 12, no. 1, pp. 13-24. https://doi.org/10.1016/S0960-9822(01)00632-7

    Paraspeckles: a novel nuclear domain. / Fox, Archa H.; Lam, Yun Wah; Leung, Anthony K. L.; Lyon, Carol E.; Andersen, Jens; Mann, Matthias; Lamond, Angus I.

    In: Current Biology, Vol. 12, No. 1, 01.2002, p. 13-24.

    Research output: Contribution to journalArticle

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    T1 - Paraspeckles: a novel nuclear domain

    AU - Fox, Archa H.

    AU - Lam, Yun Wah

    AU - Leung, Anthony K. L.

    AU - Lyon, Carol E.

    AU - Andersen, Jens

    AU - Mann, Matthias

    AU - Lamond, Angus I.

    N1 - dc.publisher: Elsevier dc.description.sponsorship: A.I.L. is a Wellcome Trust Principal Research Fellow and is funded by a Wellcome Trust Programme grant. A.H.F. is funded by a Wellcome Trust International Travelling Fellowship; A.K.L.L. is funded by a Croucher studentship; Y.W.L. is funded by a Croucher postdoctoral fellowship; and C.E.L. is funded by the Wellcome Trust. We would like to thank Dr. K. Collins for the 1787htert cell line. Work in M.M.'s laboratory is funded by a Danish National Research Foundation grant to the Centre for Experimental BioInformatics. We thank Dr. B. Frenguelli and Dr. C. Connolly from Ninewells Hospital, Dundee, for the use of the LSM510.

    PY - 2002/1

    Y1 - 2002/1

    N2 - Background: The cell nucleus contains distinct classes of subnuclear bodies, including nucleoli, splicing speckles, Cajal bodies, gems, and PML bodies. Many nuclear proteins are known to interact dynamically with one or other of these bodies, and disruption of the specific organization of nuclear proteins can result in defects in cell functions and may cause molecular disease. Results: A proteomic study of purified human nucleoli has identified novel proteins, including Paraspeckle Protein 1 (PSP1) (see accompanying article, this issue of Current Biology). Here we show that PSP1 accumulates in a new nucleoplasmic compartment, termed paraspeckles, that also contains at least two other protein components: PSP2 and p54/nrb. A similar pattern of typically 10 to 20 paraspeckles was detected in all human cell types analyzed, including primary and transformed cells. Paraspeckles correspond to discrete bodies in the interchromatin nucleoplasmic space that are often located adjacent to splicing speckles. A stable cell line expressing YFP-PSP1 has been established and used to demonstrate that PSP1 interacts dynamically with nucleoli and paraspeckles in living cells. The three paraspeckle proteins relocalize quantitatively to unique cap structures at the nucleolar periphery when transcription is inhibited. Conclusions: We have identified a novel nuclear compartment, termed paraspeckles, found in both primary and transformed human cells. Paraspeckles contain at least three RNA binding proteins that all interact dynamically with the nucleolus in a transcription-dependent fashion.

    AB - Background: The cell nucleus contains distinct classes of subnuclear bodies, including nucleoli, splicing speckles, Cajal bodies, gems, and PML bodies. Many nuclear proteins are known to interact dynamically with one or other of these bodies, and disruption of the specific organization of nuclear proteins can result in defects in cell functions and may cause molecular disease. Results: A proteomic study of purified human nucleoli has identified novel proteins, including Paraspeckle Protein 1 (PSP1) (see accompanying article, this issue of Current Biology). Here we show that PSP1 accumulates in a new nucleoplasmic compartment, termed paraspeckles, that also contains at least two other protein components: PSP2 and p54/nrb. A similar pattern of typically 10 to 20 paraspeckles was detected in all human cell types analyzed, including primary and transformed cells. Paraspeckles correspond to discrete bodies in the interchromatin nucleoplasmic space that are often located adjacent to splicing speckles. A stable cell line expressing YFP-PSP1 has been established and used to demonstrate that PSP1 interacts dynamically with nucleoli and paraspeckles in living cells. The three paraspeckle proteins relocalize quantitatively to unique cap structures at the nucleolar periphery when transcription is inhibited. Conclusions: We have identified a novel nuclear compartment, termed paraspeckles, found in both primary and transformed human cells. Paraspeckles contain at least three RNA binding proteins that all interact dynamically with the nucleolus in a transcription-dependent fashion.

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    Fox AH, Lam YW, Leung AKL, Lyon CE, Andersen J, Mann M et al. Paraspeckles: a novel nuclear domain. Current Biology. 2002 Jan;12(1):13-24. https://doi.org/10.1016/S0960-9822(01)00632-7