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Nuclear localization of the zebrafish tight junction protein nagie oko

  1. Nana Bit-Avragim1,2,
  2. Stefan Rohr1,
  3. Franziska Rudolph1,
  4. Peter Van Der Ven3,
  5. Dieter Fürst3,
  6. Jenny Eichhorst4,
  7. Burkhard Wiesner4,
  8. Salim Abdelilah-Seyfried1,*

Article first published online: 3 DEC 2007

DOI: 10.1002/dvdy.21389

Issue

Developmental Dynamics

Developmental Dynamics

Volume 237, Issue 1, pages 83–90, January 2008

Additional Information

How to Cite

Bit-Avragim, N., Rohr, S., Rudolph, F., Van Der Ven, P., Fürst, D., Eichhorst, J., Wiesner, B. and Abdelilah-Seyfried, S. (2008), Nuclear localization of the zebrafish tight junction protein nagie oko. Developmental Dynamics, 237: 83–90. doi: 10.1002/dvdy.21389

Author Information

  1. 1

    Max Delbrück Center (MDC) for Molecular Medicine, Berlin, Germany

  2. 2

    Department of Cardiology, The Charité, University Medical School of Berlin, Campus Buch, Campus Virchow Clinics, and Helios Clinics, Berlin, Germany

  3. 3

    University of Bonn, Institute of Cell Biology, Department of Molecular Cell Biology, Bonn, Germany

  4. 4

    Leipniz Institute for Molecular Pharmacology (FMP), Berlin, Germany

*Max Delbrück Center (MDC) for Molecular Medicine, Robert-Rössle Str. 10, 13125 Berlin, Germany

Publication History

  1. Issue published online: 19 DEC 2007
  2. Article first published online: 3 DEC 2007
  3. Manuscript Accepted: 22 OCT 2007

Funded by

  • Helmholtz. Grant Number: VH-VI-152

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Keywords:

  • nagie oko;
  • nuclear import;
  • nuclear export;
  • cell polarity;
  • aPKC;
  • Mpp5;
  • Pals1

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. Developmental Dynamics 237:83–90, 2008. © 2007 Wiley-Liss, Inc.

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