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- W2034156928 endingPage "193" @default.
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- W2034156928 abstract "The polypeptide ligand angiogenin, a potent inducer of angiogenesis, localizes in the nucleus/nucleolus subsequent to endocytosis by relevant cell types. This study examines the kinetic properties of the nucleolar targeting signal (NTS) of angiogenin (IMRRRGL35) at the single cell level. We show that the NTS is sufficient to target green fluorescent protein (GFP), but not β-galactosidase, to the nucleolus of rat hepatoma cells. Mutation of Arg33 to Ala within the NTS abolishes targeting activity. Nuclear/nucleolar import conferred by the NTS of angiogenin is reduced by cytosolic factors as well as ATP and is independent of importins and Ran. The NTS also confers the ability to bind to nuclear/nucleolar components which is inhibited by ATP hydrolysis; nonhydrolysable GTP analogs prevent nuclear accumulation in the absence of an intact nuclear envelope through an apparent cytoplasmic retention mechanism. Since the lectin wheat germ agglutinin does not inhibit transport, we postulate a mechanism for angiogenin nuclear/nucleolar import involving passive diffusion of angiogenin through the nuclear pore and NTS-mediated nuclear/nucleolar retention, and with cytoplasmic retention modulating the process. This pathway is clearly distinct from that of conventional signal-mediated nuclear protein import." @default.
- W2034156928 created "2016-06-24" @default.
- W2034156928 creator A5038954081 @default.
- W2034156928 creator A5070182251 @default.
- W2034156928 creator A5081382189 @default.
- W2034156928 creator A5081675173 @default.
- W2034156928 date "2001-06-01" @default.
- W2034156928 modified "2023-09-23" @default.
- W2034156928 title "Novel Properties of the Nucleolar Targeting Signal of Human Angiogenin" @default.
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- W2034156928 doi "https://doi.org/10.1006/bbrc.2001.4953" @default.
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