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Results: 7

1.
Figure 6

Figure 6. From: The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

A schematic illustration of interactome network of Odin. Protein-protein interactions indicated by black lines were those reported in the literature. Novel protein-protein interactions indicated by red lines indicate the proteins identified as components of the Odin protein complex in this study.

Jun Zhong, et al. J Proteomics. ;74(3):294-303.
2.
Figure 3

Figure 3. From: The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

Odin expression is confirmed by heavy SILAC label. MS spectra of two representative peptides from Odin are shown in panels A and C. Panels B and D show the corresponding MS/MS spectra along with the peptide sequence. * indicates 13C6-Lys or 13C6-Arg.

Jun Zhong, et al. J Proteomics. ;74(3):294-303.
3.
Figure 4

Figure 4. From: The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

Two serine phosphorylation sites identified in Odin. MS spectra of two phosphopeptides from Odin are shown in panels A and C. Panels B and D show the corresponding MS/MS spectra along with the peptide sequence. pS refers to phosphoserine. * indicates 13C6-Lys or 13C6-Arg.

Jun Zhong, et al. J Proteomics. ;74(3):294-303.
4.
Figure 5

Figure 5. From: The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

Proteins identified by the SILAC strategy. MS (panel A) and MS/MS (panel B) spectra of a representative peptide, SVDFDSLTVR, from CD2 associated protein are shown. MS (panel C) and MS/MS (panel D) spectra of a representative peptide, AIIIFVPVPQLK, from ribosomal protein S7 are shown. * indicates 13C6-Lys or 13C6-Arg.

Jun Zhong, et al. J Proteomics. ;74(3):294-303.
5.
Figure 7

Figure 7. From: The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

Validation of protein-protein interactions by co-immunoprecipitation experiments. The Odin protein complex was harvested by immunoprecipitation with anti-FLAG antibodies. The cell lysates and corresponding immunoprecipitates were resolved by SDS-PAGE and probed with antibodies against talin 2 (A), SH3KBP1 (B), CD2AP (C), ARHGAP10 (D), mortalin (E), 14-3-3ε (F), ζ (G) and γ (H).

Jun Zhong, et al. J Proteomics. ;74(3):294-303.
6.
Figure 2

Figure 2. From: The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

A schematic illustration of the SILAC methodology to identify proteins in a protein complex with Odin. Cells grown in light medium were transfected with human EGFR and empty vector as control while cells grown in heavy medium were transfected with human EGFR and FLAG-tagged Odin. Cell lysates were subjected to immunoprecipitation using anti-FLAG antibodies. After washing, the immunoprecipitates were mixed, and the bound proteins were eluted by FLAG peptides. The proteins were resolved by SDS-PAGE. The gel was stained and the protein bands excised, digested with trypsin, and analyzed by LC-MS/MS. The absence of light MS ion peak indicates a true protein interactor of Odin.

Jun Zhong, et al. J Proteomics. ;74(3):294-303.
7.
Figure 1

Figure 1. From: The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.

Tyrosine phosphorylation of Odin is induced by EGFR signaling. (A) Wild type (WT) but not kinase dead (KD) EGFR, induces tyrosine phosphorylation. Tyrosine phosphorylation status of HEK 293T cells expressing proteins the indicated constructs was assessed by Western blotting with anti-phosphotyrosine antibodies (4G10). The level of expression of WT and KD EGFR was determined by using anti-EGFR antibodies (bottom panel). (B) Odin is tyrosine phosphorylated in WT but not KD EGFR-expressing cells. Odin was immunoprecipitated from HEK 293T cells expressing the EGFR constructs as indicated in the figure. Tyrosine phosphorylation of Odin was assessed by Western blotting with anti-phosphotyrosine antibodies (4G10) and the total amount of Odin was detected by reprobing the membrane with anti-FLAG antibodies.

Jun Zhong, et al. J Proteomics. ;74(3):294-303.

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