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Author Notes:

Address correspondence to: Katharine Ullman (katharine.ullman@hci.utah.edu).

We thank Douglass Forbes for providing antibodies.

Subjects:

Research Funding:

This work was supported by National Institutes of Health Grants R01 GM61275 (K.U.) and RO1 GM059975 (M.P.) and National Institute of Child Health and Human Development intramural funds (Projects Z01 HD001902 and Z01 HD008816 to M.D.).

Shared resources used in this project are supported in part by P30 CA042014 awarded to the Huntsman Cancer Institute.

Keywords:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Cell Biology
  • CELL BIOLOGY
  • AXIN-BINDING PROTEIN
  • CELL-CYCLE
  • SUMOYLATION
  • PATHWAY
  • POM121
  • ISOPEPTIDASE
  • TRANSPORT
  • UBIQUITIN
  • MEMBRANE
  • PHOSPHORYLATION

The SUMO proteases SENP1 and SENP2 play a critical role in nucleoporin homeostasis and nuclear pore complex function

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Journal Title:

Molecular Biology of the Cell

Volume:

Volume 25, Number 1

Publisher:

, Pages 160-168

Type of Work:

Article | Final Publisher PDF

Abstract:

Nuclear pore complexes are composed of ∼30 different proteins, each present at the pore in multiple copies. Together these proteins create specialized channels that convey cargo between the cytoplasm and the nuclear interior. With the building blocks of nuclear pores identified, one challenge is to decipher how these proteins are coordinately produced and assembled into macromolecular pore structures with each cell division. Specific individual pore proteins and protein cofactors have been probed for their role in the assembly process, as well as certain kinases that add a layer of regulation via the phosphorylation status of nucleoporins. Other posttranslational modifications are candidates for coordinating events of pore assembly as well. In this study of two pore-associated small ubiquitin-like modifier (SUMO) proteases, sentrin/SUMO-specific protease 1 (SENP1) and SENP2, we observe that many nucleoporins are misloc alized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted. The pore complexes present under these conditions are still capable of transport, although the kinetics of specific cargo is altered. These results reveal a new role for the pore-associated SENPs in nucleoporin homeostasis and in achieving proper configuration of the nuclear pore complex.

Copyright information:

© 2014 Swinnen et al. This article is distributed by The American Society for Cell.

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License (http://creativecommons.org/licenses/by-nc-sa/3.0/).

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