Faculty Opinions recommendation of Tumor suppressor menin: the essential role of nuclear localization signal domains in coordinating gene expression.

2006 ◽  
Author(s):  
Patrick Gaudray
Keyword(s):  
Gene Expression ◽  
Tumor Suppressor ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Essential Role ◽  
Localization Signal

scholarly journals Tumor suppressor menin: the essential role of nuclear localization signal domains in coordinating gene expression

Oncogene ◽  
2006 ◽  
Vol 25 (25) ◽  
pp. 3537-3546 ◽  
Author(s):  
P La ◽  
A Desmond ◽  
Z Hou ◽  
A C Silva ◽  
R W Schnepp ◽  
...  
Keyword(s):  
Gene Expression ◽  
Tumor Suppressor ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Essential Role ◽  
Localization Signal

scholarly journals Dual role of the adenovirus pVI C terminus as a nuclear localization signal and activator of the viral protease

2004 ◽  
Vol 85 (11) ◽  
pp. 3367-3376 ◽  
Author(s):  
K. S. Honkavuori ◽  
B. D. Pollard ◽  
M. S. Rodriguez ◽  
R. T. Hay ◽  
G. D. Kemp
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Human Adenovirus ◽  
Dual Role ◽  
Adenovirus Infection ◽  
Heterologous Proteins ◽  
Viral Protease ◽  
C Terminus ◽  
Localization Signal

Adenain, the protease produced by adenovirus, is regulated by formation of a heterodimer with an 11 aa peptide derived from the C terminus of another adenoviral protein, pVI. Here, the role of the basic motif KRRR, which is conserved in pVI sequences from human adenovirus serotypes, was investigated. It was shown that this motif is less important than the N- or C-terminal regions in the formation of the adenain–peptide heterodimer and in the activity of the subsequent complex. This motif, however, acted as a nuclear localization signal that was capable of targeting heterologous proteins to the nucleus, resulting in a distinctive intranuclear distribution consisting of discrete foci, which is similar to that found for pVI during adenovirus infection.

scholarly journals Role of unphosphorylated, newly synthesized I kappa B beta in persistent activation of NF-kappa B.

1996 ◽  
Vol 16 (10) ◽  
pp. 5444-5449 ◽  
Author(s):  
H Suyang ◽  
R Phillips ◽  
I Douglas ◽  
S Ghosh
Keyword(s):  
Dna Binding ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Stable Complex ◽  
Dna Binding Domain ◽  
Nf Kappa B ◽  
Prolonged Stimulation ◽  
I Kappa B Alpha ◽  
Localization Signal

Stimulation with inducers that cause persistent activation of NF-kappa B results in the degradation of the NF-kappa B inhibitors, I kappa B alpha and I kappa B beta. Despite the rapid resynthesis and accumulation of I kappa B alpha, NF-kappa B remains induced under these conditions. We now report that I kappa B beta is also resynthesized in stimulated cells and appears as an unphosphorylated protein. The unphosphorylated I kappa B beta forms a stable complex with NF-kappa B in the cytosol; however, this binding fails to mask the nuclear localization signal and DNA binding domain on NF-kappa B, and the I kappa B beta-NF-kappa B complex enters the nucleus. It appears therefore that during prolonged stimulation, I kappa B beta functions as a chaperone for NF-kappa B by protecting it from I kappa B alpha and allowing it to be transported to the nucleus.

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