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  Identification of CRM1-dependent nuclear export cargos using quantitative mass spectrometry.

Thakar, K., Karaca, S., Port, S. A., Urlaub, H., & Kehlenbach, R. H. (2013). Identification of CRM1-dependent nuclear export cargos using quantitative mass spectrometry. Molecular and Cellular Proteomics, 12, 664-678. doi:10.1074/mcp.M112.024877.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-F57F-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-91C0-9
Genre: Journal Article

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 Creators:
Thakar, K., Author
Karaca, S.1, Author              
Port, S. A., Author
Urlaub, H.1, Author              
Kehlenbach, R. H., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Chromosome region maintenance 1/exportin1/Exp1/Xpo1 (CRM1) is the major transport receptor for the export of proteins from the nucleus. It binds to nuclear export signals (NESs) that are rich in leucines and other hydrophobic amino acids. The prediction of NESs is difficult because of the extreme recognition flexibility of CRM1. Furthermore, proteins can be exported upon binding to an NES-containing adaptor protein. Here we present an approach for identifying targets of the CRM1-export pathway via quantitative mass spectrometry using stable isotope labeling with amino acids in cell culture. With this approach, we identified >100 proteins from HeLa cells that were depleted from cytosolic fractions and/or enriched in nuclear fractions in the presence of the selective CRM1-inhibitor leptomycin B. Novel and validated substrates are the polyubiquitin-binding protein sequestosome 1, the cancerous inhibitor of protein phosphatase 2A (PP2A), the guanine nucleotide-binding protein-like 3-like protein, the programmed cell death protein 2-like protein, and the cytosolic carboxypeptidase 1 (CCP1). We identified a functional NES in CCP1 that mediates direct binding to the export receptor CRM1. The method will be applicable to other nucleocytoplasmic transport pathways, as well as to the analysis of nucleocytoplasmic shuttling proteins under different growth conditions.

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Language(s): eng - English
 Dates: 2012-12-132013-03-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/mcp.M112.024877
 Degree: -

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Title: Molecular and Cellular Proteomics
Source Genre: Journal
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Pages: - Volume / Issue: 12 Sequence Number: - Start / End Page: 664 - 678 Identifier: -