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GLE1  -  GLE1 RNA export mediator

Homo sapiens

Synonyms: GLE1-like protein, GLE1L, LCCS, LCCS1, Nucleoporin GLE1, ...
 
 
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High impact information on GLE1L

  • Gle1 and the phosphoinositide IP6 activate Dbp5's ATPase activity in vitro and this could provide critical spatial regulation of Dbp5 activity in vivo [1].
  • As properly processed mRNPs translocate through the pore, certain mRNP proteins are removed, probably through the enzymatic action of the DEAD-box helicase Dbp5, which binds to Nup159 and Gle1, components of the cytoplasmic filaments of the NPC [1].
  • MATERIALS AND METHODS: Two different fractions of Ganoderma lucidum extract, i.e., a fraction containing mainly polysaccharides (GLE-1), and a triterpenoid fraction without polysaccharides (GLE-2) were analyzed [2].
  • The mRNA export factor human Gle1 interacts with the nuclear pore complex protein Nup155 [3].
  • The protein Gle1 is required for export of mRNAs from the nucleus to the cytoplasm in both lower and higher eukaryotic cells [3].
 

Anatomical context of GLE1L

  • The mutual interaction between hGle1 and the symmetrically distributed nuclear pore protein Nup155 suggests a model in which hGle1's association with hNup155 may represent a step in the Gle1-mediated mRNA export pathway [3].

References

  1. Transport of messenger RNA from the nucleus to the cytoplasm. Cole, C.N., Scarcelli, J.J. Curr. Opin. Cell Biol. (2006) [Pubmed]
  2. Ganoderma lucidum extract inhibits proliferation of SW 480 human colorectal cancer cells. Xie, J.T., Wang, C.Z., Wicks, S., Yin, J.J., Kong, J., Li, J., Li, Y.C., Yuan, C.S. Experimental oncology. (2006) [Pubmed]
  3. The mRNA export factor human Gle1 interacts with the nuclear pore complex protein Nup155. Rayala, H.J., Kendirgi, F., Barry, D.M., Majerus, P.W., Wente, S.R. Mol. Cell Proteomics (2004) [Pubmed]
 
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