Proteomics

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CRM1 Exportome and nucleocytoplasmic partition

ABSTRACT: CRM1 mediates one of the major nuclear export pathways with the broadest range of cargoes. So far, more than 100 structurally and functionally diverse CRM1 cargoes have been described. We employed affinity purification mass spectrometry for in depth characterization of CRM1 "exportome" in three model systems and we identified surprisingly large numbers, namely >700 export substrates from the yeast S. cerevisiae, ≈ 1000 from Xenopus oocytes and >1050 from human cells.I. Futher, we quantified the partitioning of ≈9600 proteoforms between nucleus and cytoplasm of Xenopus oocytes.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human) Xenopus Laevis (african Clawed Frog) Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Permanent Cell Line Cell, Oocyte

SUBMITTER: Samir Karaca  

LAB HEAD: Henning Urlaub and Dirk Görlich

PROVIDER: PXD002899 | Pride | 2016-01-04

REPOSITORIES: Pride

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

Kırlı Koray K   Karaca Samir S   Dehne Heinz Jürgen HJ   Samwer Matthias M   Pan Kuan Ting KT   Lenz Christof C   Urlaub Henning H   Görlich Dirk D  

eLife 20151217

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 cont  ...[more]

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