title: A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning.
abstract: CRM1 is a highly conserved, RanGTPase-driven exportin that carries 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.
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Koray
authors.identifier: http://orcid.org/0000-0002-2289-0652
authors.initials: K
authors.lastname: Kırlı
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.|Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Samir
authors.identifier: http://orcid.org/0000-0003-4211-9053
authors.initials: S
authors.lastname: Karaca
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Heinz Jürgen
authors.identifier: http://orcid.org/0000-0002-1068-6697
authors.initials: HJ
authors.lastname: Dehne
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Matthias
authors.identifier: http://orcid.org/0000-0003-4495-8619
authors.initials: M
authors.lastname: Samwer
authors.affiliation: Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Kuan Ting
authors.identifier: http://orcid.org/0000-0001-6974-5324
authors.initials: KT
authors.lastname: Pan
authors.affiliation: Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.|Bioanalytics, Institute for Clinical Chemistry, University Medical Center Göttingen, Göttingen, Germany.
authors.forename: Christof
authors.identifier: http://orcid.org/0000-0002-0946-8166
authors.initials: C
authors.lastname: Lenz
authors.affiliation: Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.|Bioanalytics, Institute for Clinical Chemistry, University Medical Center Göttingen, Göttingen, Germany.
authors.forename: Henning
authors.identifier: http://orcid.org/0000-0003-1837-5233
authors.initials: H
authors.lastname: Urlaub
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Dirk
authors.identifier: http://orcid.org/0000-0002-4343-5210
authors.initials: D
authors.lastname: Görlich
mesh_terms: D021581:Active Transport, Cell Nucleus; D000818:Animals; D006801:Humans; D028884:Karyopherins / Q000378:metabolism*; D011506:Proteins / Q000032:analysis*; D040901:Proteomics; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*; D012441:Saccharomyces cerevisiae; D014981:Xenopus; D000097606:Exportin 1 Protein
chemical_list: D028884:Karyopherins; D011506:Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D000097606:Exportin 1 Protein
keywords: <i>s. cerevisiae</i>; NES; Nup; XPO1/CRM1; biochemistry; cell biology; exportin; human; protein localization; protein transport; xenopus