ArticleMolecular and cellular biology2008
Nuclear export receptor Xpo1/Crm1 is physically and functionally linked to the spindle pole body in budding yeast.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Therapeutic targeting of exportin-1 beyond nuclear export.Trends in pharmacological sciences · 2025Review
- Nuclear and cytoplasmic spatial protein quality control is coordinated by nuclear-vacuolar junctions and perinuclear ESCRT.Nature cell biology · 2023Article
- CRM1 Promotes Capsid Disassembly and Nuclear Envelope Translocation of Adenovirus Independently of Its Export Function.Journal of virology · 2022Article
- Therapeutic Targeting of Exportin-1 in Childhood Cancer.Cancers · 2021Review
- Screening and purification of natural products from actinomycetes that affect the cell shape of fission yeast.Journal of cell science · 2017Article
- Review
- The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal.Human molecular genetics · 2013Article
- ValidNESs: a database of validated leucine-rich nuclear export signals.Nucleic acids research · 2013Article
- Role of Mex67-Mtr2 in the nuclear export of 40S pre-ribosomes.PLoS genetics · 2012Article
- Nucleo-cytoplasmic transport of proteins and RNA in plants.Plant cell reports · 2011Review
- Article
- Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution.Biology direct · 2010Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.