Identification of a tRNA-Specific Nuclear Export Receptor

Kutay, Ulrike; Lipowsky, G.; Izaurralde, Elisa; Bischoff, F. Ralf; Schwarzmaier, Petra; Hartmann, Enno; Görlich, Dirk

doi:10.1016/s1097-2765(00)80036-2

Cited by 353 publications

(409 citation statements)

References 75 publications

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“…3 A and B). These differences also were observed with the export of several other RNAs that use other transport receptors (25,36,37). ET-202 is an artificial RNA molecule selected for its ability to be exported in the presence of the VSV M protein; it has been shown to be transported by a pathway distinct from tRNA export (25).…”

Section: A Hierarchy Of Inhibitory Activities Exists Between the Vesimentioning

confidence: 92%

Multiple vesiculoviral matrix proteins inhibit both nuclear export and import

Petersen

Her

Dahlberg

2001

Proc. Natl. Acad. Sci. U.S.A.

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The matrix (M) protein of vesicular stomatitis virus inhibits both nuclear import and export. Here, we demonstrate that this inhibitory property is conserved between the M proteins from two other vesiculoviruses, chandipura virus and spring viremia carp virus. All three M proteins completely block nuclear transport of spliced mRNA, small nuclear RNAs, and small nuclear ribonucleoproteins and slow the nuclear transport of many other cargoes. In all cases where transport was merely slowed by the M proteins, the chandipura virus M protein had the strongest inhibitory activity. When expressed in transfected HeLa cells, active M proteins displayed prominent association with the nuclear rim. Moreover, mutation of a conserved methionine abolished both the inhibitory activity and efficient targeting of the M proteins to the nuclear rim. We propose that all of the vesiculoviral M proteins associate with the same nuclear target, which is likely to be a component of the nuclear pore complex.nucleocytoplasmic transport ͉ vesiculoviruses ͉ RNA transport

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Section: A Hierarchy Of Inhibitory Activities Exists Between the Vesimentioning

confidence: 92%

Multiple vesiculoviral matrix proteins inhibit both nuclear export and import

Petersen

Her

Dahlberg

2001

Proc. Natl. Acad. Sci. U.S.A.

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“…Coupling of splicing and export of tRNA could also conveniently explain the role of two proteins, Rna1 and Los1, mutations in which resulted in the accumulation of unspliced tRNA (10,11). Rna1 protein was shown to be the GTPase activating protein (GAP) of the Ran cycle (12, 13), and Los1 protein was shown to be a tRNA exportin (14)(15)(16).…”

Section: Problems With the Classical View Of Trna Processingmentioning

confidence: 99%

Have tRNA, will travel

Phizicky

2005

Proc. Natl. Acad. Sci. U.S.A.

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“…In the case of nuclear export, several mediators have been studied to date. They include the importin ␣ export factors (human CAS and yeast Cse1) (10 -12), tRNA export factors (human Xpo-t and yeast Los1) (13)(14)(15), and NES 1 export factors (human Crm1 and yeast Xpo1) (16 -19). The transport machinery is remarkably versatile, with individual karyopherins recognizing multiple cargoes and with individual cargoes binding to multiple karyopherins (see reviews, Refs.…”

mentioning

confidence: 99%

Conformational Variability of Nucleo-cytoplasmic Transport Factors

Fukuhara

Fernández

Ebert

et al. 2004

Journal of Biological Chemistry

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The transport of macromolecules between the nucleus and cytoplasm of eukaryotic cells is largely mediated by a single family of transport factors, the karyopherin or importin ␤-like family. Structural and biochemical evidence suggests conformational flexibility of these modular HEAT-repeat proteins is crucial for their regulation. Here we use small angle x-ray scattering to assess the extent of conformational variation within a set of nuclear import and export factors. The study reveals that importin ␤, transportin, and the exportin Xpo-t share a similar S-like superhelical conformation in their unbound state. There are no obvious differences in the overall structures that might generally distinguish nuclear export from nuclear import mediators. Two other members of the family, the exportins Cse1 and Xpo1, possess a significantly more globular conformation, indicating that the extended S-like architecture is not a hallmark of all karyopherins. Binding of RanGTP/cargo to importin ␤, transportin, and Xpo-t triggers distinct conformational responses, suggesting that even closely related karyopherins employ different mechanisms of conformational regulation and that cargo and nuclear pore-interacting surfaces of the different receptors may be unique.Nucleo-cytoplasmic transport factors of the karyopherin ␤ family shuttle through nuclear pore complexes spanning the nuclear envelope and mediate the nuclear import and/or export of specific protein or RNA cargoes (for review, see Refs.

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Identification of a tRNA-Specific Nuclear Export Receptor

Cited by 353 publications

References 75 publications

Multiple vesiculoviral matrix proteins inhibit both nuclear export and import

Multiple vesiculoviral matrix proteins inhibit both nuclear export and import

Have tRNA, will travel

Conformational Variability of Nucleo-cytoplasmic Transport Factors

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