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The authors determined the crystal structure of a conserved domain in the carboxy-terminal tail of lamins that is not present in cytoplasmic intermediate filaments. The domain is a non-standard immunoglobulin fold and is the site of many mutations, some of which cause either Emery-Dreifuss muscular dystrophy or familial partial lipodystrophy.
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This is the first paper showing that lamins can assemble into stable 10 nm filaments in vitro. This has important implications for the structure of the lamina.
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Liu J., Ben-Shahar T.R., Riemer D., Treinin M., Spann P., Weber K., Fire A., Gruenbaum Y. Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol. Biol. Cell. 11:2000;3937-3947.
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Nili E., Cojocaru G.S., Kalma Y., Ginsberg D., Copeland N.G., Gilbert D.J., Jenkins N.A., Berger R., Shaklai S., Amariglio N.et al. Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less). J. Cell Sci. 114:2001;3297-3307.
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The disruption of lamin organization with a dominant-negative mutant lamin specifically blocks RNA polymerase II activity in cultured cells and in cell-free preparations of Xenopus nuclei.
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Spann T.P., Goldman A.E., Wang C., Huang S., Goldman R.D. Alteration of nuclear lamin organization inhibits RNA polymerase II- dependent transcription. J. Cell Biol. 156:2002;603-608 The disruption of lamin organization with a dominant-negative mutant lamin specifically blocks RNA polymerase II activity in cultured cells and in cell-free preparations of Xenopus nuclei.
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41
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This is a thought-provoking article indicating that there are forms of lamins in spliceosomes. This suggests that lamin structure changes depending on the location within the nucleus.
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Kumaran R.I., Muralikrishna B., Parnaik V.K. Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription. J. Cell Biol. 159:2002;783-793 This is a thought-provoking article indicating that there are forms of lamins in spliceosomes. This suggests that lamin structure changes depending on the location within the nucleus.
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Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr
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HIV-1 Vpr induces a localized reduction of lamins at the nuclear periphery and this is related to the formation of blebs. These burst frequently and reseal, allowing nuclear proteins to enter the cytoplasm and vice versa. This cycle of bleb formation and bursting may be involved in Vpr-induced G2 cell cycle arrest.
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de Noronha C.M., Sherman M.P., Lin H.W., Cavrois M.V., Moir R.D., Goldman R.D., Greene W.C. Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr. Science. 294:2001;1105-1108 HIV-1 Vpr induces a localized reduction of lamins at the nuclear periphery and this is related to the formation of blebs. These burst frequently and reseal, allowing nuclear proteins to enter the cytoplasm and vice versa. This cycle of bleb formation and bursting may be involved in Vpr-induced G2 cell cycle arrest.
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