Structural basis for the assembly of a nuclear export complex

@article{Matsuura2004StructuralBF,
  title={Structural basis for the assembly of a nuclear export complex},
  author={Yoshiyuki Matsuura and Murray Stewart},
  journal={Nature},
  year={2004},
  volume={432},
  pages={872-877}
}
The nuclear import and export of macromolecular cargoes through nuclear pore complexes is mediated primarily by carriers such as importin-β. Importins carry cargoes into the nucleus, whereas exportins carry cargoes to the cytoplasm. Transport is orchestrated by nuclear RanGTP, which dissociates cargoes from importins, but conversely is required for cargo binding to exportins. Here we present the 2.0 Å crystal structure of the nuclear export complex formed by exportin Cse1p complexed with its… 
Structural basis for nuclear import complex dissociation by RanGTP
TLDR
The structure of full-length yeast importin- β (Kap95p or karyopherin-β) complexed with RanGTP is presented, which provides a basis for understanding the crucial cargo-release step of nuclear import.
Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP
TLDR
The structure of an exportin complex shows how nuclear transport complexes differentially recognize cargo and suggests that RanGTP promotes cargo-binding to CRM1 solely through long-range conformational changes in the exportin.
Structural basis for the nuclear protein import cycle.
  • M. Stewart
  • Biology, Chemistry
    Biochemical Society transactions
  • 2006
TLDR
Crystallography and biochemical and cellular studies have enabled a molecular description of the transport cycle to be developed and tested using protein engineering and computer modelling.
Mechanistic Insights from Structural Analyses of Ran-GTPase-Driven Nuclear Export of Proteins and RNAs.
  • Y. Matsuura
  • Biology, Chemistry
    Journal of molecular biology
  • 2016
Allosteric control of the exportin CRM1 unraveled by crystal structure analysis
TLDR
Detailed understanding of the flexibility, the regulatory features and the positive binding cooperativity between CRM1, Ran and cargo is a prerequisite for the development of highly effective drugs.
Nuclear export of actin: A biochemical and structural perspective
TLDR
A new single-step protocol for purification of profilin*β/γ-actin complexes from cytoplasmic extracts, which enabled us to purify a stable actin export complex and crystallize the actin nuclear export complex, which was successfully crystallized.
Structures of Importins and Exportins
TLDR
Nucleotide-specific conformational differences of the Ran GTPase, structural information on importin-α and of ten different Kaps describing how each protein recognizes cargo(s), how Ran affects Kap-cargo interactions, and in a few cases how Kaps interact with nucleoporins are covered.
Ran‐dependent nuclear export mediators: a structural perspective
TLDR
The current state of knowledge is reviewed and emerging principles as well as prevailing questions about RanGTPase‐dependent export mediators are highlighted.
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