The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

GLE2  -  RNA export factor GLE2

Saccharomyces cerevisiae S288c

Synonyms: Nuclear pore protein GLE2, Nucleoporin GLE2, RAE1, YER107C, poly(A) RNA export protein RAE1
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of GLE2

  • We found that an mRNA export factor Gle2p rapidly dissociated from the nuclear envelope and diffused into the cytoplasm at 42 degrees C. However, in exponential phase cells pretreated with mild heat stress (37 degrees C for 1 h), Gle2p did not dissociate at 42 degrees C, and the export of bulk poly(A)(+) mRNA continued [1].

High impact information on GLE2

  • Gle2p is anchored at the nuclear envelope (NE) via a short Gle2p-binding motif within Nup116p called GLEBS [2].
  • Gle2p is implicated in nuclear export of poly(A)+ RNA and nuclear pore complex (NPC) structure and distribution in Saccharomyces cerevisiae [2].
  • Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p [3].
  • Using the GFP-Nup49p system with a mutant in the NPC-associated factor Gle2p that exhibits formation of NPC clusters only at 37 degrees C, it was possible to distinguish between these two models for NPC dynamics [4].
  • The dissociation of Gle2p was caused by increased membrane fluidity and correlated closely with blocking of the export of bulk poly(A)(+) mRNA [1].

Biological context of GLE2


Anatomical context of GLE2


Physical interactions of GLE2

  • Thus, the in vivo function of Gle2p is strictly coupled to the short GLEBS within Nup116p which links this putative mRNA transport factor to the nuclear pores [3].
  • A ptr1-1 rae1-167 double mutant showed a synthetic effect on a growth defect, indicating that Ptr1p functionally interacts with an essential mRNA export factor Rae1p [7].

Other interactions of GLE2

  • Gle2p physically associated with Nup116p in vitro, and the interaction required the N-terminal region of Nup116p [8].
  • By fluorescence-activated cell sorting for cells with low GFP signal from a population of mutagenized cells expressing GFP-Nup49p, three complementation groups were identified: two correspond to mutant nup120 and gle2 alleles that result in clusters of NPCs [9].
  • With regard to genetic specificity, the nup116-C lethality was also suppressed by high-copy GLE2 and NIC96 [8].
  • Interestingly, a two-hybrid interaction was detected between Gle2p and Srp1p, the nuclear localization signal receptor, as well as Rip1p, a nuclear export signal-interacting protein [10].
  • Comparison of the Bub3 sequence to the WD40 protein, Rae1, shows high sequence conservation along the same surfaces [11].

Analytical, diagnostic and therapeutic context of GLE2


  1. Gle2p is essential to induce adaptation of the export of bulk poly(A)+ mRNA to heat shock in Saccharomyces cerevisiae. Izawa, S., Takemura, R., Inoue, Y. J. Biol. Chem. (2004) [Pubmed]
  2. RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. Pritchard, C.E., Fornerod, M., Kasper, L.H., van Deursen, J.M. J. Cell Biol. (1999) [Pubmed]
  3. Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p. Bailer, S.M., Siniossoglou, S., Podtelejnikov, A., Hellwig, A., Mann, M., Hurt, E. EMBO J. (1998) [Pubmed]
  4. In vivo dynamics of nuclear pore complexes in yeast. Bucci, M., Wente, S.R. J. Cell Biol. (1997) [Pubmed]
  5. The mitotic checkpoint protein hBUB3 and the mRNA export factor hRAE1 interact with GLE2p-binding sequence (GLEBS)-containing proteins. Wang, X., Babu, J.R., Harden, J.M., Jablonski, S.A., Gazi, M.H., Lingle, W.L., de Groen, P.C., Yen, T.J., van Deursen, J.M. J. Biol. Chem. (2001) [Pubmed]
  6. Aging in check. Dai, W., Wang, X. Science of aging knowledge environment [electronic resource] : SAGE KE (2006) [Pubmed]
  7. The fission yeast ptr1+ gene involved in nuclear mRNA export encodes a putative ubiquitin ligase. Andoh, T., Azad, A.K., Shigematsu, A., Ohshima, Y., Tani, T. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  8. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Ho, A.K., Raczniak, G.A., Ives, E.B., Wente, S.R. Mol. Biol. Cell (1998) [Pubmed]
  9. A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly. Bucci, M., Wente, S.R. Mol. Biol. Cell (1998) [Pubmed]
  10. GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function. Murphy, R., Watkins, J.L., Wente, S.R. Mol. Biol. Cell (1996) [Pubmed]
  11. Crystal structure of the spindle assembly checkpoint protein Bub3. Larsen, N.A., Harrison, S.C. J. Mol. Biol. (2004) [Pubmed]
WikiGenes - Universities