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CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals
TLDR
It is concluded that CRM1 is an export receptor for leucine-rich nuclear export signals and a model for the role of RanGTP inCRM1 function and in nuclear export in general is discussed. Expand
Nucleocytoplasmic transport: the soluble phase.
TLDR
Directionality of either import or export depends on association between a substrate and its receptor on one side of the nuclear envelope and dissociation on the other, and the Ran GTPase is critical in generating this asymmetry. Expand
The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
The GTPase Ran is essential for nuclear import of proteins with a classical nuclear localization signal (NLS). Ran's nucleotide‐bound state is determined by the chromatin‐bound exchange factor RCC1Expand
The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly
TLDR
A stepwise model is proposed in which postmitotic NPC assembly initiates on chromatin via early recruitment of the Nup107-160 complex, which is conserved in higher eukaryotes and prevents association of FG-repeat nucleoporins with chromatin. Expand
PHAX, a Mediator of U snRNA Nuclear Export Whose Activity Is Regulated by Phosphorylation
TLDR
This work identifies PHAX (phosphorylated adaptor for RNA export) as the additional factor required for U snRNA export complex assembly in vitro and shows that the compartmentalized PHAx phosphorylation cycle can contribute to the directionality of export. Expand
HURP Is Part of a Ran-Dependent Complex Involved in Spindle Formation
TLDR
HURP is a new and essential component of the mitotic apparatus and acts as part of a multicomponent complex that affects the growth or stability of spindleMTs and is required for spindle MT organization. Expand
Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway
TLDR
It is proposed that ICP27 associates with viral mRNAs and recruits TAP/NXF1 via its interaction with REF proteins, allowing the otherwise inefficiently exported viral m RNAs to access the TAP‐mediated export pathway. Expand
Ran Induces Spindle Assembly by Reversing the Inhibitory Effect of Importin α on TPX2 Activity
TLDR
It is shown that components of the nuclear transport machinery serve to regulate spindle formation in M phase, and TPX2 is required for Ran.GTP, a microtubule-associated protein previously known to target a motor protein, Xklp2, to microtubules. Expand
Dominant‐negative mutants of importin‐β block multiple pathways of import and export through the nuclear pore complex
TLDR
These importin‐β mutants are very efficient inhibitors of NLS‐dependent protein import, however, they also inhibit M9 signal‐mediated nuclear import as well as nuclear export of mRNA, U snRNA, and the NES‐containing Rev protein, which suggests that mediators of these various transport events share binding sites on the NPC and/or that mechanisms exist to coordinate translocation through the NPC via different nucleocytoplasmic transport pathways. Expand
Dominant‐negative mutants of importin‐β block multiple pathways of import and export through the nuclear pore complex
Nuclear protein import proceeds through the nuclear pore complex (NPC). Importin‐β mediates translocation via direct interaction with NPC components and carries importin‐α with the NLS substrate fromExpand
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