Proteomic Identification of Common SCF Ubiquitin Ligase FBXO6-Interacting Glycoproteins in Three kinds of Cells

FBOX6 ubiquitin ligase complex is involved in the endoplasmic reticulum-associated degradation pathway by mediating the ubiquitination of glycoproteins. FBXO6 interacts with the chitobiose in unfolded N-glycoprotein, pointing glycoproteins toward E2 for ubiquitination. Although the glycoprotein-reco...

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Bibliographic Details
Published in:Journal of proteome research 2012-03, Vol.11 (3), p.1773-1781
Main Authors: Liu, Bin, Zheng, Ying, Wang, Tong-Dan, Xu, Han-Zhang, Xia, Li, Zhang, Jian, Wu, Ying-Li, Chen, Guo-Qiang, Wang, Li-Shun
Format: Article
Language:English
Subjects:
Cullin Proteins - metabolism
Glycoproteins - isolation & purification
Glycoproteins - metabolism
HEK293 Cells
HeLa Cells
Humans
Jurkat Cells
Membrane Glycoproteins - metabolism
Oxidoreductases - metabolism
Protein Binding
Protein Interaction Mapping
Protein Interaction Maps
Proteomics
SKP Cullin F-Box Protein Ligases - metabolism
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Summary:FBOX6 ubiquitin ligase complex is involved in the endoplasmic reticulum-associated degradation pathway by mediating the ubiquitination of glycoproteins. FBXO6 interacts with the chitobiose in unfolded N-glycoprotein, pointing glycoproteins toward E2 for ubiquitination. Although the glycoprotein-recognizing mechanism of FBXO6 is well documented, its bona fide interacting glycoproteins are largely unknown. Here we utilized a protein purification approach combined with LC–MS to systematically identify the FBXO6-interacting glycoproteins. Following identification of 39 proteins that specifically interact with FBXO6 in all three different cell lines, 293T, HeLa and Jurkat cells, we compared the protein complex organization between wild-type FBXO6 and its mutant, which fails to recognize glycoproteins. Combining these databases, 29 highly confident glycoproteins that interact with FBXO6 in an N-glycan dependent manner are identified. Our data provide valuable information for the discovery of the interacting glycoproteins of FBXO6 and also demonstrate the potential of these approaches as general platforms for the global discovery of interacting glycoproteins of other FBAs (F-box associated regions) containing F-box proteins.
ISSN:1535-3893
1535-3907
DOI:10.1021/pr2010204