Cited by 919Nuclear Structure and FunctionMicrotubule and mitosis dynamicsProtein Structure and Dynamics

Molecular mechanism of the nuclear protein import cycle

Stewart, Murray·2007·Nature Reviews Molecular Cell Biology

Abstract

The nuclear import of proteins through nuclear pore complexes (NPCs) illustrates how a complex biological function can be generated by a spatially and temporally organized cycle of interactions between cargoes, carriers and the Ran GTPase. Recent work has given considerable insight into this process, especially about how interactions are coordinated and the basis for the molecular recognition that underlies the process. Although considerable progress has been made in identifying and characterizing the molecular interactions in the soluble phase that drive the nuclear protein import cycle, understanding the precise mechanism of translocation through NPCs remains a major challenge.

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Crossref · 10.1038/nrm2114

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  • In the absence of sumoylation, RanGAP1 is unable to bind RanBP2 or localize to the nuclear envelope.

    “In the absence of sumoylation, RanGAP1 is unable to bind RanBP2 or localize to the nuclear envelope (Figure 4C, (31–33).”
  • Importin-α acts as an adaptor protein that recognizes the NLS of cargo proteins and is transported as a ternary complex with importin-β into the nucleus.

    “Importin-α is a constituent of the classical nuclear import pathway. It acts as an adaptor protein that recognizes the NLS of cargo proteins and is transported as a ternary complex with importin-β into the nucleus [39], [40]”
  • Cargo protein with a classic NLS requires a direct interaction with importin-α to be transported through the nuclear pore complex.

    “Cargo protein with a classic NLS requires a direct interaction with importin-α to be transported through the nuclear pore complex [31], [40], [45], [46], [47]”
  • Transportation of cargo protein in importin-α/−β protein complexes through the NPC requires energy derived from the activities of GTPases.

    “Transportation of cargo protein in importin-α/−β protein complexes through the NPC requires energy derived from the activities of GTPases [40], [45] (Figure 2A).”

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Authors
Stewart, M.
Affiliations
MRC Laboratory of Molecular Biology (GB)
Corresponding author
Stewart, Murray
Venue
Nature Reviews Molecular Cell Biology
Published
2007-02-07
Volume
8
Issue
3
Pages
195-208
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
OpenAlex
W2048492672
Cited by
919
References
101
Citations by year
2026: 28 · 2025: 38 · 2024: 33 · 2023: 50 · 2022: 43 · 2021: 37 · 2020: 51 · 2019: 50 · 2018: 37 · 2017: 42 · 2016: 53 · 2015: 51 · 2014: 54 · 2013: 42 · 2012: 36
FWCI
5.79
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Reviews Molecular Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
nuclear protein import, Ran GTPase, nuclear pore complex, nuclear import receptor, molecular recognition, nuclear transport
MeSH terms
Animals, Cell Nucleus, Models, Molecular, Nuclear Proteins, ran GTP-Binding Protein, Protein Transport, Active Transport, Cell Nucleus, Nuclear Pore Complex Proteins

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