Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore

Xun X Bao, Christos Spanos, Tomoko Kojidani, Eric M Lynch, Juri Rappsilber, Yasushi Hiraoka, Tokuko Haraguchi, Kenneth E Sawin

Research output: Contribution to journalArticlepeer-review

Abstract

Non-centrosomal microtubule organizing centers (MTOCs) are important for microtubule organization in many cell types. In fission yeast Schizosaccharomyces pombe, the protein Mto1, together with partner protein Mto2 (Mto1/2 complex), recruits the g-tubulin complex to multiple non-centrosomal MTOCs, including the nuclear envelope (NE). Here, we develop a comparative-interactome mass spectrometry approach to determine how Mto1 localizes to the NE. Surprisingly, we find that Mto1, a constitutively cytoplasmic protein, docks at nuclear pore complexes (NPCs), via interaction with exportin Crm1 and cytoplasmic FG-nucleoporin Nup146. Although Mto1 is not a nuclear export cargo, it binds Crm1 via a nuclear export signal-like sequence, and docking requires both Ran in the GTP-bound state and Nup146 FG repeats. In addition to determining the mechanism of MTOC formation at the NE, our results reveal a novel role for Crm1 and the nuclear export machinery in the stable docking of a cytoplasmic protein complex at NPCs.

Original languageEnglish
Number of pages34
JournaleLIFE
Volume7
DOIs
Publication statusPublished - 29 May 2018

Keywords

  • S. pombe
  • cell biology
  • exportin
  • microtubule
  • microtubule organizing center
  • nuclear pore

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