Words similar to nucleocytoplasmic
Example sentences for: nucleocytoplasmic
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Other tab mutants (such as tab3, TAB5, CDC14 TAB 6and TAB7 ) showed no defect in this assay, suggesting that bypass of cdc15Δ can be achieved without perturbing nucleocytoplasmic transport.
AtCOP1 contains three conserved structural domains: a RING finger at the amino terminus, a coiled-coil domain in the middle, and a carboxyl-terminal WD40 repeat domain [ 9 10 ] . Each of the three conserved domains has been shown to mediate protein-protein interactions [ 11 12 13 ] . The subcellular localization of AtCOP1 is regulated by light in a tissue specific manner [ 14 15 ] . The hypocotyl cell nuclei contain high levels of COP1 in the dark and reduced levels in the light, suggesting that the nucleocytoplasmic partitioning of AtCOP1 is adjusted by a light-responsive mechanism [ 14 16 ] . The activity of AtCOP1 is at least in part regulated by its subcellular localization, as the degradation of HY5 is dependent upon the nuclear accumulation of AtCOP1 in the dark [ 4 ] . AtCOP1 was demonstrated to carry a single, bipartite nuclear localization signal located between the coiled-coil domain and the WD-40 domain (amino acid 294-314) and a cytoplasmic localization signal, which was mapped to a region partially overlapping with the RING finger and the coiled-coil domain (amino acid 67-117) [ 17 ] . Strikingly, AtCOP1 protein forms characteristic nuclear speckles when transiently expressed in onion epidermal cells or stably expressed in transgenic Arabidopsis [ 6 18 ] . The functional role of these speckles is currently unknown; however, a subnuclear localization signal consisting of 58 residues (amino acid 120-177) is required for their formation [ 19 ] .
The subcellular localization of AtCOP1 is regulated by light [ 14 ] , a feature that is critical for its function [ 4 29 ] . Interestingly, the localization of mammalian COP1 protein expressed in plant cells can also be regulated by light [ 20 ] , implicating a similar mechanism may operate for the nucleocytoplasmic partitioning of COP1 in mammalian cells.
One attractive hypothesis based on our identification of MTR10 as a tab gene is that MEN proteins regulate the nucleocytoplasmic distribution of a key regulator of the release process.
Multiple tabmutations influence nucleocytoplasmic transport
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