TY - JOUR
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.
U2 - 10.1016/S0960-9822(01)00632-7
DO - 10.1016/S0960-9822(01)00632-7
M3 - Article
SN - 1879-0445
VL - 12
SP - 13
EP - 24
JO - Current Biology
JF - Current Biology
IS - 1
ER -