Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore.
Elife
; 72018 05 29.
Article
em En
| MEDLINE
| ID: mdl-29809148
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 γ-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.
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Base de dados:
MEDLINE
Assunto principal:
Schizosaccharomyces
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Receptores Citoplasmáticos e Nucleares
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Poro Nuclear
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Centro Organizador dos Microtúbulos
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Carioferinas
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Microtúbulos
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article