ArticleStructure (London, England : 1993)2015
Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Visualizing nuclear pore complex plasticity with pan-expansion microscopy.The Journal of cell biology · 2025Article
- Visualizing nuclear pore complex plasticity with pan-Expansion Microscopy.bioRxiv : the preprint server for biology · 2025Article
- Importin α/β and the tug of war to keep TDP-43 in solution: quo vadis?BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Review
- Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022Review
- A role for Nup153 in nuclear assembly reveals differential requirements for targeting of nuclear envelope constituents.Molecular biology of the cell · 2022Article
- Recognition of the TDP-43 nuclear localization signal by importin α1/β.Cell reports · 2022Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Differential recognition of canonical NF-κB dimers by Importin α3.Nature communications · 2022Article
- A distinct inner nuclear membrane proteome in Saccharomyces cerevisiae gametes.G3 (Bethesda, Md.) · 2021Article
- Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-α.Viruses · 2020Article
- Ran pathway-independent regulation of mitotic Golgi disassembly by Importin-α.Nature communications · 2019Article
- Mapping the native organization of the yeast nuclear pore complex using nuclear radial intensity measurements.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Identification of the evolutionarily conserved nuclear envelope proteins Lem2 and MicLem2 inGene: X · 2019Article
- Systematic analysis of NLMP suggests nuclear localization of RTK/MET kinases resemble cancer cell clearance.Journal of experimental & clinical cancer research : CR · 2019Article
- Nup2 performs diverse interphase functions in Aspergillus nidulans.Molecular biology of the cell · 2018Article
- Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1.Nature communications · 2017Article
- Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.The Journal of biological chemistry · 2016Article
- PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage.Nucleic acids research · 2016Article
- Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Targeting of ER-synthesized membrane proteins to the inner nuclear membrane (INM) has long been explained by the diffusion-retention model. However, several INM proteins contain non-classical nuclear localization signal (NLS) sequences, which, in a few instances, have been shown to promote importin α/β- and Ran-dependent translocation to the INM. Here, using structural and biochemical methods, we show that yeast INM proteins Heh2 and Src1/Heh1 contain bipartite import sequences that associate intimately with the minor NLS-binding pocket of yeast importin α and unlike classical NLSs efficiently displace the IBB domain in the absence of importin β. In vivo, the intimate interactions at the minor NLS-binding pocket make the h2NLS highly efficient at recruiting importin α at the ER and drive INM localization of endogenous Heh2. Thus, h1/h2NLSs delineate a novel class of super-potent, IBB-like membrane protein NLSs, distinct from classical NLSs found in soluble cargos and of general interest in biology.
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