Projects per year
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.
- S. pombe
- cell biology
- microtubule organizing center
- nuclear pore
FingerprintDive into the research topics of 'Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore'. Together they form a unique fingerprint.
1/12/12 → 30/11/14
Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore
Bao, X. (Creator), Spanos, C. (Creator), Kojidani, T. (Creator), Lynch, E. M. (Creator), Rappsilber, J. (Creator), Hiraoka, Y. (Creator), Haraguchi, T. (Creator) & Sawin, K. (Creator), PRIDE database hosted by European Bioinformatics Institute, EBI, 22 May 2018