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  A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning.

Kirli, K., Karaca, S., Dehne, H. J., Samwer, M., Pan, K. T., Lenz, C., et al. (2015). A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning. eLife, 4: e11466. doi:10.7554/eLife.11466.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-5415-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-CA76-A
Genre: Journal Article

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http://elifesciences.org/content/4/e11466v4 (Publisher version)
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 Creators:
Kirli, K.1, Author              
Karaca, S.2, Author              
Dehne, H. J.1, Author              
Samwer, M., Author
Pan, K. T.2, Author              
Lenz, C.2, Author              
Urlaub, H.2, Author              
Görlich, D.1, Author              
Affiliations:
1Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society, ou_578574              
2Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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Free keywords: S. cerevisiae; biochemistry; cell biology; human; xenopus
 Abstract: CRM1 is a highly conserved, RanGTPase-driven exportin that caries proteins and RNPs from the nucleus to the cytoplasm. We now explored the cargo-spectrum of CRM1 in depth and identified surprisingly large numbers, namely >700 export substrates from the yeast S. cerevisiae, ≈ 1000 from Xenopus oocytes and >1050 from human cells. In addition, we quantified the partitioning of ≈5000 unique proteins between nucleus and cytoplasm of Xenopus oocytes. The data suggest new CRM1 functions in spatial control of vesicle coat-assembly, centrosomes, autophagy, peroxisome biogenesis, cytoskeleton, ribosome maturation, translation, mRNA degradation, and more generally in precluding a potentially detrimental action of cytoplasmic pathways within the nuclear interior. There are also numerous new instances where CRM1 appears to act in regulatory circuits. Altogether, our dataset allows unprecedented insights into the nucleocytoplasmic organisation of eukaryotic cells, into the contributions of an exceedingly promiscuous exportin and it provides a new basis for NES prediction.

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Language(s): eng - English
 Dates: 2015-12-17
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.11466
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Title: eLife
Source Genre: Journal
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Pages: 28 Volume / Issue: 4 Sequence Number: e11466 Start / End Page: - Identifier: -