ArticlePloS one2015
Crystal structure of human importin-α1 (Rch1), revealing a potential autoinhibition mode involving homodimerization.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- Toxoplasma Gondii Importin α Shows Weak Auto-Inhibition.The protein journal · 2023Article
- Deciphering the Binding of the Nuclear Localization Sequence of Myc Protein to the Nuclear Carrier Importin α3.International journal of molecular sciences · 2022Article
- Article
- Recognition of the TDP-43 nuclear localization signal by importin α1/β.Cell reports · 2022Article
- Invasion and Propagation of White Spot Syndrome Virus: Hijacking of the Cytoskeleton, Intracellular Transport Machinery, and Nuclear Import Transporters.Journal of virology · 2022Article
- Interaction of spindle assembly factor TPX2 with importins-α/β inhibits protein phase separation.The Journal of biological chemistry · 2021Article
- The Paralogue of the Intrinsically Disordered Nuclear Protein 1 Has a Nuclear Localization Sequence that Binds to Human Importin α3.International journal of molecular sciences · 2020Article
- A Phosphorylation-Induced Switch in the Nuclear Localization Sequence of the Intrinsically Disordered NUPR1 Hampers Binding to Importin.Biomolecules · 2020Article
- Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-α.Viruses · 2020Article
- Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses.Nature communications · 2018Article
- A motif within the armadillo repeat of Parkinson's-linked LRRK2 interacts with FADD to hijack the extrinsic death pathway.Scientific reports · 2018Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we determined the crystal structure of N-terminal importin-β-binding domain (IBB)-truncated human importin-α1 (ΔIBB-h-importin-α1) at 2.63 Å resolution. The crystal structure of ΔIBB-h-importin-α1 reveals a novel closed homodimer. The homodimer exists in an autoinhibited state in which both the major and minor nuclear localization signal (NLS) binding sites are completely buried in the homodimerization interface, an arrangement that restricts NLS binding. Analytical ultracentrifugation studies revealed that ΔIBB-h-importin-α1 is in equilibrium between monomers and dimers and that NLS peptides shifted the equilibrium toward the monomer side. This finding suggests that the NLS binding sites are also involved in the dimer interface in solution. These results show that when the IBB domain dissociates from the internal NLS binding sites, e.g., by binding to importin-β, homodimerization possibly occurs as an autoinhibition state.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.