scholarly journals Erratum: Structural basis for leucine-rich nuclear export signal recognition by CRM1

Nature ◽  
2009 ◽  
Vol 461 (7263) ◽  
pp. 550-550
Author(s):  
Xiuhua Dong ◽  
Anindita Biswas ◽  
Katherine E. Süel ◽  
Laurie K. Jackson ◽  
Rita Martinez ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Structural Basis ◽  
Signal Recognition ◽  
Export Signal

scholarly journals Structural basis for leucine-rich nuclear export signal recognition by CRM1

Nature ◽  
2009 ◽  
Vol 458 (7242) ◽  
pp. 1136-1141 ◽  
Author(s):  
Xiuhua Dong ◽  
Anindita Biswas ◽  
Katherine E. Süel ◽  
Laurie K. Jackson ◽  
Rita Martinez ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Structural Basis ◽  
Signal Recognition ◽  
Export Signal

scholarly journals Altered Nuclear Export Signal Recognition as a Driver of Oncogenesis

2019 ◽  
Vol 9 (10) ◽  
pp. 1452-1467 ◽  
Author(s):  
Justin Taylor ◽  
Maria Sendino ◽  
Alexander N. Gorelick ◽  
Alessandro Pastore ◽  
Matthew T. Chang ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Signal Recognition ◽  
Export Signal

scholarly journals Biogenesis of the Signal Recognition Particle (Srp) Involves Import of Srp Proteins into the Nucleolus, Assembly with the Srp-Rna, and Xpo1p-Mediated Export

2001 ◽  
Vol 153 (4) ◽  
pp. 745-762 ◽  
Author(s):  
Helge Grosshans ◽  
Karina Deinert ◽  
Ed Hurt ◽  
George Simos
Keyword(s):  
Nuclear Export ◽  
Protein Import ◽  
Signal Recognition Particle ◽  
Nuclear Export Signal ◽  
Secretory Proteins ◽  
Signal Recognition ◽  
Core Proteins ◽  
Import Receptors ◽  
Export Signal ◽  
Srp Rna

The signal recognition particle (SRP) targets nascent secretory proteins to the ER, but how and where the SRP assembles is largely unknown. Here we analyze the biogenesis of yeast SRP, which consists of an RNA molecule (scR1) and six proteins, by localizing all its components. Although scR1 is cytoplasmic in wild-type cells, nuclear localization was observed in cells lacking any one of the four SRP “core proteins” Srp14p, Srp21p, Srp68p, or Srp72p. Consistently, a major nucleolar pool was detected for these proteins. Sec65p, on the other hand, was found in both the nucleoplasm and the nucleolus, whereas Srp54p was predominantly cytoplasmic. Import of the core proteins into the nucleolus requires the ribosomal protein import receptors Pse1p and Kap123p/Yrb4p, which might, thus, constitute a nucleolar import pathway. Nuclear export of scR1 is mediated by the nuclear export signal receptor Xpo1p, is distinct from mRNA transport, and requires, as evidenced by the nucleolar accumulation of scR1 in a dis3/rrp44 exosome component mutant, an intact scR1 3′ end. A subset of nucleoporins, including Nsp1p and Nup159p (Rat7p), are also necessary for efficient translocation of scR1 from the nucleus to the cytoplasm. We propose that assembly of the SRP requires import of all SRP core proteins into the nucleolus, where they assemble into a pre-SRP with scR1. This particle can then be targeted to the nuclear pores and is subsequently exported to the cytoplasm in an Xpo1p-dependent way.

scholarly journals Characterization of the Interaction between the Interferon-Induced Protein P56 and the Int6 Protein Encoded by a Locus of Insertion of the Mouse Mammary Tumor Virus

2000 ◽  
Vol 74 (4) ◽  
pp. 1892-1899 ◽  
Author(s):  
Jinjiao Guo ◽  
Ganes C. Sen
Keyword(s):  
Nuclear Export ◽  
Nuclear Protein ◽  
Nuclear Export Signal ◽  
Structural Basis ◽  
Specific Domain ◽  
Interacting Protein ◽  
Amino Terminal ◽  
Tumor Virus ◽  
Export Signal ◽  
Two Hybrid

ABSTRACT For determining cellular functions of the interferon-inducible human cytoplasmic protein P56, we undertook a Saccharomyces cerevisiae two-hybrid screen that identified Int6 as a P56-interacting protein. That the interaction also occurs in human cells was confirmed by coimmunoprecipitation and the observed cytoplasmic displacement of nuclear Int6 upon coexpression of P56. Because Int6 has been claimed to be both a cytoplasmic and a nuclear protein, we investigated the structural basis of this discrepancy. By mutational analyses, we showed that the Int6 protein contains a bipartite nuclear localization signal and a nuclear export signal at the far end of the amino terminus. The 20 amino-terminal residues of Int6, when they were attached to a different nuclear protein, were sufficient to translocate that protein to the cytoplasm. Within this region, replacement of any of the three leucine residues with alanine destroyed the function of the export signal. The specific domain of P56 that is required for its interaction with Int6 was mapped using the yeast two-hybrid assay and a mammalian coimmunoprecipitation assay. Both assays demonstrated that the C-terminal region of P56 containing three specific tetratricopeptide motifs is required for this interaction. In contrast, removal of an internal domain of P56 enhanced the interaction, as quantified by the two-hybrid assay.

The Structure of BRMS1 Nuclear Export Signal and SNX6 Interacting Region Reveals a Hexamer Formed by Antiparallel Coiled Coils

2011 ◽  
Vol 411 (5) ◽  
pp. 1114-1127 ◽  
Author(s):  
Mercedes Spínola-Amilibia ◽  
José Rivera ◽  
Miguel Ortiz-Lombardía ◽  
Antonio Romero ◽  
José L. Neira ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Coiled Coils ◽  
Export Signal

scholarly journals Nuclear Export of L-Periaxin, Mediated by Its Nuclear Export Signal in the PDZ Domain

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e91953 ◽  
Author(s):  
Yawei Shi ◽  
Lei Zhang ◽  
Ting Yang
Keyword(s):  
Nuclear Export ◽  
Pdz Domain ◽  
Nuclear Export Signal ◽  
Export Signal

scholarly journals Properties of Two EBV Mta Nuclear Export Signal Sequences

Virology ◽  
2001 ◽  
Vol 288 (1) ◽  
pp. 119-128 ◽  
Author(s):  
Lin Chen ◽  
Gangling Liao ◽  
Masahiro Fujimuro ◽  
O.John Semmes ◽  
S.Diane Hayward
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Signal Sequences ◽  
Export Signal

scholarly journals OsWRKY62 and OsWRKY76 interact with Importin α1s for Negative Regulation of Defensive Responses in Nucleus

2021 ◽  
Author(s):  
Xiaohui Xu ◽  
Han Wang ◽  
Jiqin Liu ◽  
Shuying Han ◽  
Miaomiao Lin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nuclear Localization ◽  
Nuclear Export ◽  
Nuclear Translocation ◽  
Nuclear Export Signal ◽  
Defense Responses ◽  
Nuclear Localization Signals ◽  
Defensive Responses ◽  
Export Signal ◽  
Positively Charged

Abstract Background: OsWRKY62 and OsWRKY76, two close members of WRKY transcription factors, function together as transcriptional repressors. OsWRKY62 is predominantly localized in the cytosol. What are the regulatory factors for OsWRKY62 nuclear translocation?Results: In this study, we characterized they interacted with rice importin, OsIMα1a and OsIMα1b, for nuclear translocation. Chimeric OsWRKY62.1-GFP, which is predominantly localized in the cytoplasm, was translocated to the nucleus of Nicotiana benthamiana leaf cells in the presence of OsIMα1a or OsIMαDIBB1a lacking the auto-inhibitory importin β-binding domain. OsIMαDIBB1a interacted with the WRKY domain of OsWRKY62.1, which has specific bipartite positively charged concatenated amino acids functioning as a nuclear localization signal. Similarly, we found that OsIMαDIBB1a interacted with the AvrPib effector of rice blast fungus Magnaporthe oryzae, which contains a scattered distribution of positively charged amino acids. Furthermore, we identified a nuclear export signal in OsWRKY62.1 that inhibited nuclear transportation. Overexpression of OsIMα1a or OsIMα1b enhanced resistance to M. oryzae, whereas knockout mutants decreased resistance to the pathogen. However, overexpressing both OsIMα1a and OsWRKY62.1 were slightly more susceptible to M. oryzae than OsWRKY62.1 alone. Ectopic overexpression of OsWRKY62.1 with an extra nuclear export signal compromised the enhanced susceptibility of OsWRKY62.1 to M. oryzae.Conclusion: These results indicated that OsWRKY62 localization is a consequence of competition binding between rice importins and exportins. OsWRKY62, OsWRKY76, and AvrPib effector translocate to nucleus in association with importin α1s through new types of nuclear localization signals for negatively regulating defense responses.

scholarly journals Structural determinants of nuclear export signal orientation in binding to exportin CRM1

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Ho Yee Joyce Fung ◽  
Szu-Chin Fu ◽  
Chad A Brautigam ◽  
Yuh Min Chook
Keyword(s):  
Crystal Structures ◽  
Nuclear Export ◽  
Chromosome Region ◽  
Nuclear Export Signal ◽  
Opposite Orientation ◽  
Structural Determinants ◽  
Large Expansion ◽  
Export Signal

The Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of hundreds of proteins through recognition of their nuclear export signals (NESs), which are highly variable in sequence and structure. The plasticity of the CRM1-NES interaction is not well understood, as there are many NES sequences that seem incompatible with structures of the NES-bound CRM1 groove. Crystal structures of CRM1 bound to two different NESs with unusual sequences showed the NES peptides binding the CRM1 groove in the opposite orientation (minus) to that of previously studied NESs (plus). Comparison of minus and plus NESs identified structural and sequence determinants for NES orientation. The binding of NESs to CRM1 in both orientations results in a large expansion in NES consensus patterns and therefore a corresponding expansion of potential NESs in the proteome.

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