Nucleocytoplasmic transport: the soluble phase
Abstract
Active transport between the nucleus and cytoplasm involves primarily three classes of macromolecules: substrates, adaptors, and receptors. Some transport substrates bind directly to an import or an export receptor while others require one or more adaptors to mediate formation of a receptor-substrate complex. Once assembled, these transport complexes are transferred in one direction across the nuclear envelope through aqueous channels that are part of the nuclear pore complexes (NPCs). Dissociation of the transport complex must then take place, and both adaptors and receptors must be recycled through the NPC to allow another round of transport to occur. Directionality of either import or export therefore depends on association between a substrate and its receptor on one side of the nuclear envelope and dissociation on the other. The Ran GTPase is critical in generating this asymmetry. Regulation of nucleocytoplasmic transport generally involves specific inhibition of the formation of a transport complex; however, more global forms of regulation also occur.
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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]”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [39]
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LEDGF/p75 Is Essential for Nuclear and Chromosomal Targeting of HIV-1 Integrase in Human Cells
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A Conserved mRNA Export Machinery Coupled to pre-mRNA Splicing
Reed, R., & Hurt, E. (2002) · Cell · doi:10.1016/s0092-8674(02)00627-x · Cited by 400 · see citing works
The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP
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Stress-mediated nuclear stabilization of p53 is regulated by ubiquitination and importin-α3 binding
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Nup153 unlocks the nuclear pore complex for HIV-1 nuclear translocation in nondividing cells
Buffone, C., Martinez-Lopez, A., Fricke, T., Opp, S., Severgnini, M., Cifola, I., Petiti, L., Frabetti, S., Skorupka, K., Zadrozny, K. K., et al. (2018) · Journal of Virology · doi:10.1128/jvi.00648-18 · Cited by 109 · see citing works
tRNAs promote nuclear import of HIV-1 intracellular reverse transcription complexes
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UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner
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“transported as a ternary complex with importin-b into the nucleus [39,40] (Figure 2A).”
Background
- Authors
- Mattaj, I. W., & Englmeier, L.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1998-06
- Volume
- 67
- Issue
- 1
- Pages
- 265-306
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2151298994
- Cited by
- 1,175
- References
- 303
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 8 · 2023: 14 · 2022: 13 · 2021: 7 · 2020: 11 · 2019: 12 · 2018: 13 · 2017: 14 · 2016: 12 · 2015: 11 · 2014: 24 · 2013: 26 · 2012: 27
- FWCI
- 9.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- nuclear transport, nuclear import, nuclear export, nuclear pore complex, Ran GTPase, transport receptors, transport regulation, nuclear envelope
- MeSH terms
- Biological Transport, Active, Cell Nucleus, Cytoplasm, Nuclear Envelope, Solubility, Cell Polarity, Receptors, Cytoplasmic and Nuclear, Nuclear Localization Signals
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