Dissection of a Nuclear Localization Signal
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TL;DR: The energetic details of NLS recognition by the receptor importin α through quantitative analysis of variant NLSs are decoded to generate an energetic scale of nuclear localization sequences based on a peptide's affinity for the importinα-importin β complex.
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About: This article is published in Journal of Biological Chemistry. The article was published on 12 Jan 2001. and is currently open access. The article focuses on the topics: Nuclear localization sequence & Importin.
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Citations
Classical Nuclear Localization Signals: Definition, Function, and Interaction with Importin α
Allison Lange,Ryan E. Mills,Christopher J. Lange,Murray Stewart,Scott E. Devine,Anita H. Corbett +5 more
TL;DR: The best understood system for the transport of macromolecules between the cytoplasm and the nucleus is the classical nuclear import pathway and a bioinformatics approach is taken to analyze the likely prevalence of this system in vivo.
1.2K
Molecular mechanism of the nuclear protein import cycle
TL;DR: The nuclear import of proteins through nuclear pore complexes (NPCs) illustrates how a complex biological function can be generated by a spatially and temporally organized cycle of interactions between cargoes, carriers and the Ran GTPase.
951
Six Classes of Nuclear Localization Signals Specific to Different Binding Grooves of Importin α
Shunichi Kosugi,Masako Hasebe,Nobutaka Matsumura,Hideaki Takashima,Etsuko Miyamoto-Sato,Masaru Tomita,Hiroshi Yanagawa +6 more
TL;DR: Six different NLS classes that specifically bind to distinct binding pockets of importin α are reported, finding that they fundamentally require the regions outside the core basic residues for their activity and have specific residues or patterns that confer the activities differently between yeast, plants, and mammals.
635
Molecular basis for specificity of nuclear import and prediction of nuclear localization
Mary Marfori,Andrew V. Mynott,Jonathan Ellis,Ahmed M. Mehdi,Neil F. W. Saunders,Paul M. G. Curmi,Jade K. Forwood,Mikael Bodén,Bostjan Kobe,Bostjan Kobe +9 more
TL;DR: In this paper, the authors review the current understanding of the molecular determinants of the specificity of nuclear import, focusing on the importin-α•cargo recognition, as well as the currently available databases and predictive tools relevant to nuclear localization.
426
Nuclear Localization of Peptidylarginine Deiminase V and Histone Deimination in Granulocytes
TL;DR: The results suggested that the NLS is a classical monopartite NLS, which is not found in the three other PADs and may have implications in histone modifications.
392
References
Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
Michael Rexach,Günter Blobel +1 more
TL;DR: It is proposed that movement of NLS proteins across the nuclear pore complex is a stochastic process that operates via repeated association-dissociation reactions.
810
Structure of importin-beta bound to the IBB domain of importin-alpha.
TL;DR: The crystal structure indicates that significant conformational changes occur when importin-β binds or releases the IBB domain domain and suggests how dissociation of the importIn-α/β heterodimer may be achieved upon nuclear entry.
571
The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex.
TL;DR: The cDNA deduced primary structure of a wheat germ agglutinin-reactive nuclear pore complex (NPC) protein of rat is reported and it is suggested that bidirectional transport across the NPC proceeds by repeated docking and undocking reactions.
478
Development of the multiple sequence approximation within the AGADIR model of α‐helix formation: Comparison with Zimm‐Bragg and Lifson‐Roig formalisms
Victor Muñoz,Luis Serrano +1 more
TL;DR: The comparison between AGADIRms and the Lifson-Roig formalism shows that, despite the differences on treating helix/coil cooperativity, both theories give virtually identical results when an equivalent set of parameters is used.
426
Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha.
TL;DR: The structure of mouse importin α has been determined and explains the regulatory switch between the cytoplasmic, high-affinity form, and the nuclear, low-Affinity form for NLS binding of the nuclear import receptor predicted by the current models of nuclear import.
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