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The Times. Forbes Publishing. Financial Post. Postmedia Network. Retrieved 6 August Retrieved 25 January Retrieved 12 March Herald Sun. The Herald and Weekly Times. Deutsche Welle. Retrieved 23 June Apple's big enemy in smartphone wars: Retrieved 1 September The challenge now is to understand the kinetic differences governing the nuclear import of classical, non-classical and IBB-like import sequences and how this may affect the efficiency and energetic requirement for movement through the NPC. We thank Adem Koksal and Anshul Bhardwaj for critical reading of the manuscript. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication.

As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

National Center for Biotechnology Information , U. Biochim Biophys Acta. Author manuscript; available in PMC Sep 1. Kaylen Lott 1 Dept.

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Gino Cingolani 1 Dept. Author information Copyright and License information Disclaimer. Gino Cingolani, Ph. Copyright notice. The publisher's final edited version of this article is available at Biochim Biophys Acta. See other articles in PMC that cite the published article.

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Abstract Specific and efficient recognition of import cargoes is essential to ensure nucleocytoplasmic transport. Introduction 1. Open in a separate window. Design Principles of Nucleocytoplasmic Transport Transport across the nuclear envelope is an active, receptor-mediated process, which is essential for normal cell function reviewed in [ 14 — 21 ]. Role of the IBB-domain in import complex assembly 3. Footnotes Publisher's Disclaimer: References 1. Sequence requirements for nuclear location of simian virus 40 large-T antigen. A short amino acid sequence able to specify nuclear location.

Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Nuclear targeting signal recognition: Sessler RJ, Noy N. A ligand-activated nuclear localization signal in cellular retinoic acid binding protein-II.

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Mol Cell. The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import. EMBO J. Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure. Structure of importin-beta bound to the IBB domain of importin-alpha. Molecular basis for the recognition of snurportin 1 by importin beta.

J Biol Chem. Siomi H, Dreyfuss G. A nuclear localization domain in the hnRNP A1 protein.

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  • J Cell Biol. Rules for nuclear localization sequence recognition by karyopherin beta 2. Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta. Gorlich D, Kutay U. Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol. The yeast nuclear pore complex: Virtual gating and nuclear transport: Trends Cell Biol.

    Fried H, Kutay U. Nucleocytoplasmic transport: Cell Mol Life Sci. Peters R. Translocation through the nuclear pore complex: Dynamic nuclear pore complexes: Weis K. The nuclear pore complex: Biology and biophysics of the nuclear pore complex and its components. Int Rev Cell Mol Biol. Fahrenkrog B, Aebi U. Nat Rev Mol Cell Biol. Drummond S, Allen T. Structure, function and assembly of the nuclear pore complex. Symp Soc Exp Biol. Structure, dynamics and function of nuclear pore complexes. Nuclear pore complex biogenesis. Curr Opin Cell Biol. The nuclear pore complex has entered the atomic age.

    Disorder in the nuclear pore complex: Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Bischoff FR, Gorlich D. FEBS Lett. Mosammaparast N, Pemberton LF. Classical nuclear localization signals: Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Requirement of guanosine triphosphate-bound ran for signal-mediated nuclear protein export. Moroianu J, Blobel G. Nachury MV, Weis K. The direction of transport through the nuclear pore can be inverted.

    Importin alpha: Evidence for distinct substrate specificities of importin alpha family members in nuclear protein import. Mol Cell Biol. Meyer T, Vinkemeier U. Nucleocytoplasmic shuttling of STAT transcription factors. Eur J Biochem. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat Struct Mol Biol. Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport. Evolutionary specialization of the nuclear targeting apparatus. J Mol Biol. Karyopherin flexibility in nucleocytoplasmic transport.

    Curr Opin Struct Biol. Stewart M. Molecular mechanism of the nuclear protein import cycle. Chook YM, Blobel G. Karyopherins and nuclear import. Structural biology of nucleocytoplasmic transport. Annu Rev Biochem. Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. Cell Cycle. Andrade MA, Bork P. HEAT repeats in the Huntington's disease protein. Nat Genet. Will CL, Luhrmann R.

    Spliceosomal UsnRNP biogenesis, structure and function. Structural basis for leucine-rich nuclear export signal recognition by CRM1. Wold MS. Replication protein A: Kobe B. Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha.

    The Importin β Binding Domain as a Master Regulator of Nucleocytoplasmic Transport

    Nat Struct Biol. Quantitative analysis of nuclear localization signal NLS -importin alpha interaction through fluorescence depolarization. Evidence for auto-inhibitory regulation of NLS binding. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Conti E, Kuriyan J. Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha. Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha.

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    • Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha. Phospholipid scramblase 1 contains a nonclassical nuclear localization signal with unique binding site in importin alpha. Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-alpha using oriented peptide library screening. Dissection of a nuclear localization signal.

      Characterization of the auto-inhibitory sequence within the N-terminal domain of importin alpha. The auto-inhibitory function of importin alpha is essential in vivo. Biophysical characterization of interactions involving importin-alpha during nuclear import. Molecular basis for the recognition of phosphorylated STAT1 by importin a5. Mol Biology. Conformational variability of nucleocytoplasmic transport factors. Zachariae U, Grubmuller H. Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association.

      Bhardwaj A, Cingolani G. Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains. Matsuura Y, Stewart M. Structural basis for the assembly of a nuclear export complex.