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Mol Biol Cell
2002 Feb 01;132:425-34. doi: 10.1091/mbc.01-06-0308.
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Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm.
Panté N
,
Kann M
.
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Bidirectional transport of macromolecules between the nucleus and the cytoplasm occurs through the nuclear pore complexes (NPCs) by a signal-mediated mechanism that is directed by targeting signals (NLSs) residing on the transported molecules or "cargoes." Nuclear transport starts after interaction of the targeting signal with soluble cellular receptors. After the formation of the cargo-receptor complex in the cytosol, this complex crosses the NPC. Herein, we use gold particles of various sizes coated with cargo-receptor complexes to determine precisely how large macromolecules crossing the NPC by the signal-mediated transport mechanism could be. We found that cargo-receptor-gold complexes with diameter close to 39 nm could be translocated by the NPC. This implies that macromolecules much larger than the assumed functional NPC diameter of 26 nm can be transported into the karyoplasm. The physiological relevance of this finding was supported by the observation that intact nucleocapsids of human hepatitis B virus with diameters of 32 and 36 nm are able to cross the nuclear pore without disassembly.
Akey,
Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy.
1993, Pubmed,
Xenbase
Akey,
Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy.
1993,
Pubmed
,
Xenbase
Baschong,
Small colloidal gold conjugated to Fab fragments or to immunoglobulin G as high-resolution labels for electron microscopy: a technical overview.
1990,
Pubmed
Catimel,
Biophysical characterization of interactions involving importin-alpha during nuclear import.
2001,
Pubmed
Chook,
Pictures in cell biology. Structures of nuclear-transport components.
1999,
Pubmed
Cingolani,
Structure of importin-beta bound to the IBB domain of importin-alpha.
1999,
Pubmed
Conti,
Nucleocytoplasmic transport enters the atomic age.
2001,
Pubmed
Conti,
Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha.
1998,
Pubmed
Crowther,
Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy.
1994,
Pubmed
De Robertis,
Intracellular migration of nuclear proteins in Xenopus oocytes.
1978,
Pubmed
,
Xenbase
Dingwall,
A polypeptide domain that specifies migration of nucleoplasmin into the nucleus.
1982,
Pubmed
,
Xenbase
Dworetzky,
The effects of variations in the number and sequence of targeting signals on nuclear uptake.
1988,
Pubmed
,
Xenbase
Feldherr,
Movement of a karyophilic protein through the nuclear pores of oocytes.
1984,
Pubmed
,
Xenbase
Görlich,
Isolation of a protein that is essential for the first step of nuclear protein import.
1994,
Pubmed
,
Xenbase
Görlich,
Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope.
1995,
Pubmed
,
Xenbase
Hinshaw,
Architecture and design of the nuclear pore complex.
1992,
Pubmed
,
Xenbase
Horisberger,
Colloidal gold, a useful marker for transmission and scanning electron microscopy.
1977,
Pubmed
Kann,
Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus.
1994,
Pubmed
Kann,
In vitro model for the nuclear transport of the hepadnavirus genome.
1997,
Pubmed
Kann,
Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex.
1999,
Pubmed
Kasamatsu,
How do animal DNA viruses get to the nucleus?
1998,
Pubmed
Kenney,
Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores.
1995,
Pubmed
Mattaj,
Nucleocytoplasmic transport: the soluble phase.
1998,
Pubmed
Moroianu,
Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes.
1995,
Pubmed
Nakielny,
Transport of proteins and RNAs in and out of the nucleus.
1999,
Pubmed
Paine,
Nuclear envelope permeability.
1975,
Pubmed
Panté,
The nuclear pore complex.
1993,
Pubmed
Panté,
Visualizing nuclear export of different classes of RNA by electron microscopy.
1997,
Pubmed
,
Xenbase
Radu,
Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins.
1995,
Pubmed
,
Xenbase
Ribbeck,
Kinetic analysis of translocation through nuclear pore complexes.
2001,
Pubmed
Richardson,
Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translocation through nuclear pores.
1988,
Pubmed
,
Xenbase
Slot,
A new method of preparing gold probes for multiple-labeling cytochemistry.
1985,
Pubmed
Stoffler,
The nuclear pore complex: from molecular architecture to functional dynamics.
1999,
Pubmed
Wente,
Gatekeepers of the nucleus.
2000,
Pubmed
Whittaker,
Viral entry into the nucleus.
2000,
Pubmed
Whittaker,
Nuclear import and export of viruses and virus genomes.
1998,
Pubmed
Wrigley,
The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy.
1968,
Pubmed
