NLS-mediated NPC functions of the nucleoporin Pom121

FEBS Lett. 2010 Aug 4;584(15):3292-8. doi: 10.1016/j.febslet.2010.07.008. Epub 2010 Jul 14.

Abstract

RanGTP mediates nuclear import and mitotic spindle assembly by dissociating import receptors from nuclear localization signal (NLS) bearing proteins. We investigated the interplay between import receptors and the transmembrane nucleoporin Pom121. We found that Pom121 interacts with importin alpha/beta and a group of nucleoporins in an NLS-dependent manner. In vivo, replacement of Pom121 with an NLS mutant version resulted in defective nuclear transport, induction of aberrant cytoplasmic membrane stacks and decreased cell viability. We propose that the NLS sites of Pom121 affect its function in NPC assembly both by influencing nucleoporin interactions and pore membrane structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Survival
  • Humans
  • Kinetics
  • Membrane Glycoproteins / metabolism*
  • Mutant Proteins / metabolism
  • Mutation / genetics
  • Nuclear Envelope / metabolism
  • Nuclear Envelope / ultrastructure
  • Nuclear Localization Signals / metabolism*
  • Nuclear Pore / metabolism*
  • Nuclear Pore Complex Proteins / metabolism*
  • Protein Binding
  • Protein Transport
  • Structure-Activity Relationship
  • Xenopus
  • Xenopus Proteins / metabolism*
  • beta Karyopherins / metabolism

Substances

  • Membrane Glycoproteins
  • Mutant Proteins
  • Nuclear Localization Signals
  • Nuclear Pore Complex Proteins
  • POM121 protein, human
  • Pom121 protein, Xenopus
  • Xenopus Proteins
  • beta Karyopherins