Tyrosine Phosphorylation of the Gα-Interacting Protein GIV Promotes Activation of Phosphoinositide 3-Kinase During Cell Migration

Changsheng Lin, Jason Ear, Yelena Pavlova, Yash Mittal, Irina Kufareva, Majid Ghassemian, Ruben Abagyan, Mikel Garcia-Marcos, Pradipta Ghosh*

*To whom correspondence should be addressed. E-mail: prghosh{at}ucsd.edu

This PDF file includes:

• Fig. S1. GIV is phosphorylated in vitro by receptor tyrosine kinases and in cells in response to growth factors.
• Fig. S2. Bioinformatic analyses of the phosphopeptide sequences of GIV.
• Fig. S3. Both EGFR and Src can phosphorylate GIV after EGF stimulation.
• Fig. S4. The GEF domain is not required for tyrosine phosphorylation of GIV.
• Fig. S5. GIV interacts with p85α and EGFR upon growth factor stimulation.
• Fig. S6. Molecular modeling of the interfaces between the SH2 domains of p85α and the GIV-derived phosphopeptides.
• Fig. S7. PIP₃ production and localization as detected by a Btk-based reporter.
• pTyrGIVCT file description
• References

[Download PDF]

Technical Details

Format: Adobe Acrobat PDF

Size: 1.22 MB

Other Supplementary Material for this manuscript includes the following:

• pTyrGIVCT files

[Download pTyrGIVCT files (Compressed)]

Technical Details

Format: Microsoft Excel. Files are packaged as a compressed archive, in *.zip format; users should download the compressed file to their machine and decompress the file on their local hard drive, using the instructions below.

Size: 6.62 MB (compressed); 12.8 MB (decompressed)

Instructions for downloading and decompressing files:

1. Create a temporary folder on your machine's hard drive.
2. Save the compressed archive to the temporary folder you created, using the links above.
3. Decompress the compressed file in the temporary folder using decompression software such as WinZip (Windows; www.winzip.com) or StuffIt Expander (Windows and Mac; www.stuffit.com).

© 2011 American Association for the Advancement of Science