English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons179664

Kirli,  K.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons85360

Karaca,  S.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons188191

Dehne,  H. J.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons185577

Pan,  K. T.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons85543

Lenz,  C.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15132

Görlich,  D.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

External Resource
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-5415-C
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.