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


ABSTRACT: The spindle pole body (SPB) represents the microtubule organizing center in the budding yeast Saccharomyces cerevisiae. It is a highly structured organelle embedded in the nuclear membrane, which is required to anchor microtubules 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 SPB. 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.

SUBMITTER: Neuber A 

PROVIDER: S-EPMC2519715 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature

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

Neuber Anja A   Franke Jacqueline J   Wittstruck Angelika A   Schlenstedt Gabriel G   Sommer Thomas T   Stade Katrin K  

Molecular and cellular biology 20080623 17


The spindle pole body (SPB) represents the microtubule organizing center in the budding yeast Saccharomyces cerevisiae. It is a highly structured organelle embedded in the nuclear membrane, which is required to anchor microtubules 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  ...[more]

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