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 FAK nuclear export signal sequences

FEBS Letters ◽  
2008 ◽  
Vol 582 (16) ◽  
pp. 2402-2406 ◽  
Author(s):  
Valeria Ossovskaya ◽  
Ssang-Taek Lim ◽  
Nobuyuki Ota ◽  
David D. Schlaepfer ◽  
Dusko Ilic
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Signal Sequences ◽  
Export Signal

Nuclear export of α-catenin: overlap between nuclear export signal sequences and the β-catenin binding site

2004 ◽  
Vol 295 (1) ◽  
pp. 150-160 ◽  
Author(s):  
Ana Giannini ◽  
Michal Mazor ◽  
Mariam Orme ◽  
Maria Vivanco ◽  
Jonathan Waxman ◽  
...  
Keyword(s):  
Binding Site ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Signal Sequences ◽  
Export Signal

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 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.

scholarly journals Regulation of intracellular dynamics of Smad4 by its leucine‐rich nuclear export signal

EMBO Reports ◽  
2000 ◽  
Vol 1 (2) ◽  
pp. 176-182 ◽  
Author(s):  
Mina Watanabe ◽  
Norihisa Masuyama ◽  
Makoto Fukuda ◽  
Eisuke Nishida
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Export Signal
Sign in / Sign up

Export Citation Format

Share Document