ZFIN ID: ZDB-PUB-071210-33
Nuclear localization of the zebrafish tight junction protein nagie oko
Bit-Avragim, N., Rohr, S., Rudolph, F., Van Der Ven, P., Fürst, D., Eichhorst, J., Wiesner, B., and Abdelilah-Seyfried, S.
Date: 2008
Source: Developmental dynamics : an official publication of the American Association of Anatomists   237(1): 83-90 (Journal)
Registered Authors: Abdelilah-Seyfried, Salim
Keywords: nagie oko, nuclear import, nuclear export, cell polarity, aPKC, Mpp5, Pals1
MeSH Terms:
  • Amino Acid Motifs/genetics
  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Cell Nucleus/metabolism*
  • Cell Polarity/genetics
  • Computational Biology
  • Epithelial Cells/metabolism
  • Guanylate Cyclase/genetics
  • Guanylate Cyclase/metabolism*
  • Humans
  • Immunohistochemistry
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Kinase C-alpha/genetics
  • Protein Kinase C-alpha/metabolism
  • Protein Transport
  • Sequence Homology, Amino Acid
  • Zebrafish/genetics
  • Zebrafish/metabolism*
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed: 18058913 Full text @ Dev. Dyn.
FIGURES
ABSTRACT
The tight junctions-associated MAGUK protein nagie oko is closely related to Drosophila Stardust, mouse protein associated with lin-seven 1 (Pals1), and human MAGUK p55 subfamily member 5 (Mpp5). As a component of the evolutionarily conserved Crumbs protein complex, nagie oko is essential for the maintenance of epithelial cell polarity. Here, we show that nagie oko contains a predicted nuclear export and two conserved nuclear localization signals. We find that loss of the predicted nuclear export signal results in nuclear protein accumulation. We show that nagie oko nuclear import is redundantly controlled by the two nuclear localization signals and the evolutionarily conserved region 1 (ECR1), which links nagie oko with Par6-aPKC. Finally, deletion forms of nagie oko that lack nuclear import and export signals complement several nagie oko mutant defects in cell polarity and epithelial integrity. This finding provides an entry point to potentially novel and unknown roles of this important cell polarity regulator.
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