The nuclear export receptor Xpo1/Crm1 is physically and functionally linked to the spindle pole body in budding yeast

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Item Type:	Article
Title:	The nuclear export receptor Xpo1/Crm1 is physically and functionally linked to the spindle pole body in budding yeast
Creators Name:	Neuber, A., Franke, J., Wittstruck, A., Schlenstedt, G., Sommer, T. and Stade, K.
Abstract:	The spindle pole body (SPB) represents the microtubule organizing center in budding yeast. It is a highly structured organelle embedded in the nuclear membrane which is required to anchor microtubules (MTs) on both sides of the nuclear envelope. The protein Spc72, a component of the SPB, is located at the cytoplasmic face of this organelle and serves as a receptor for the gamma-tubulin complex. In this paper we show that it is also a binding partner of the nuclear export receptor Xpo1/Crm1. Xpo1 binds its cargoes in a Ran-dependent fashion via a short leucine-rich nuclear export signal (NES). We show that binding of Spc72 to Xpo1 depends on Ran-GTP and a functional NES in Spc72. Mutations in this NES have severe consequences for mitotic spindle morphology in vivo. This is also the case for xpo1 mutants, which show a reduction in cytoplasmic microtubules. In addition, we find a subpopulation of Xpo1 localized at the spindle pole body. Based on these data, we propose a functional link between Xpo1 and the SPB and discuss a role for this exportin in spindle biogenesis in budding yeast.
Keywords:	Cell Nucleus Active Transport, Cell Nucleus, Guanosine Triphosphate, Karyopherins, Microtubule-Associated Proteins, Microtubules, Mitotic Spindle Apparatus, Monomeric GTP-Binding Proteins, Mutation, Nuclear Export Signals, Nuclear Proteins, Peptide Fragments, Protein Binding, Protein Transport, Cytoplasmic and Nuclear Receptors, Saccharomyces Cerevisiae, Saccharomyces Cerevisiae Proteins
Source:	Molecular and Cellular Biology
ISSN:	0270-7306
Publisher:	American Society for Microbiology
Volume:	28
Number:	17
Page Range:	5348-5358
Date:	September 2008
Official Publication:	https://doi.org/10.1128/MCB.02043-07
PubMed:	View item in PubMed

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