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| Open AccessCo-translational binding of importins to nascent proteins
Importins are known to facilitate nucleocytoplasmic transport and cytoplasmic chaperoning of some proteins. Here, the authors uncover that these proteins also act as co-translational chaperones for specific sets of proteins, for example ribonucleic acid binding factors.
- Maximilian Seidel
- , Natalie Romanov
- & Martin Beck
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Article
| Open AccessDifferential recognition of canonical NF-κB dimers by Importin α3
Nuclear translocation of the p50/p65 heterodimer is essential for NF-κB signaling. Here, the authors identify a bipartite Nuclear Localization Signal in the NF-κB p50/p65 heterodimer that is recognized with high affinity by importin α3.
- Tyler J. Florio
- , Ravi K. Lokareddy
- & Gino Cingolani
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Article
| Open AccessNuclear transporter Importin-13 plays a key role in the oxidative stress transcriptional response
Importin superfamily member IPO13 mediates nuclear transport bidirectionally. Here the authors delineate the transcriptome of wild-type and IPO13-knockout mouse embryonic stem cells, revealing IPO13’s key role in the oxidative stress response through targeted transport of specific transcription factors.
- K. A. Gajewska
- , H. Lescesen
- & D. A. Jans
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Article
| Open AccessRan pathway-independent regulation of mitotic Golgi disassembly by Importin-α
Golgi disassembly is required for mitosis and occurs by vesicle fusion suppression, although the mechanism is unclear. Here, Chang et al. show, with quantitative analyses and crystallography, that Importin-α regulates this process by blocking GM130-p115 interactions in a Ran pathway-independent way.
- Chih-Chia Chang
- , Ching-Jou Chen
- & Kuo-Chiang Hsia
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Article
| Open AccessStructural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses
Importin α isoforms regulate the nuclear import of different cargo proteins but the mechanisms conferring isoform specificity are not fully understood. Here, the authors study the interactions of importin α1 and α3 with two viral cargos, elucidating the structural basis for isoform-specific cargo recognition.
- Kate M. Smith
- , Sofiya Tsimbalyuk
- & Jade K. Forwood
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Article
| Open AccessThree-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1
Importin α3 facilitates the nuclear transport of the Ran guanine nucleotide exchange factor RCC1. Here the authors reveal the molecular basis for the selectivity of RCC1 for importin α3 vs the generic importin α1 and discuss the evolution of importin α isoforms.
- Rajeshwer S. Sankhala
- , Ravi K. Lokareddy
- & Gino Cingolani
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Article
| Open AccessOM14 is a mitochondrial receptor for cytosolic ribosomes that supports co-translational import into mitochondria
Mitochondrial proteins can be imported post-translationally; however, a role for co-translational import has recently provoked renewed interest. Lesnik et al.identify OM14 as a mitochondrial ribosome receptor required for efficient co-translational import of mitochondrial proteins.
- Chen Lesnik
- , Yifat Cohen
- & Yoav Arava