Phospholipase C-gamma 1 binds to actin-cytoskeleton via its C-terminal SH2 domain in vitro

Biochemical and Biophysical Research Communications
Z PeiJ R Williamson

Abstract

Association of phospholipase C (PLC)-gamma 1 with the cytoskeleton has been postulated to be one of the crucial steps for PLC-gamma 1 activation and translocation to the plasma membrane. In this report, direct binding assays were carried out to study which fragment of PLC-gamma 1 Src homology region has been able to bind to the actin-cytoskeleton. Using GST fusion proteins containing various deletions of the PLC-gamma 1 Src homology region, it was found that PLC-gamma 1 binds to the actin-cytoskeleton directly via its C-terminal SH2 domain but not the SH3 domain in vitro. However, the binding of the C-terminal SH2 domain of PLC-gamma 1 to actin did not interfere with the SH2 domain's ability to associate with phosphotyrosine, which suggested that actin and phosphotyrosine residues may bind to different sequences in the C-terminal SH2 domain of PLC-gamma 1.

Citations

Oct 22, 2003·The Journal of Cell Biology·Yong-Kook KwonMichel Bernier
Jun 18, 2016·Experimental & Molecular Medicine·Jung Min HaSun Sik Bae
Oct 26, 2000·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·S Nojiri, J B Hoek
Oct 9, 1999·The Journal of Biological Chemistry·B N KholodenkoJ B Hoek
Nov 18, 2009·The Journal of Immunology : Official Journal of the American Association of Immunologists·Esteban CarrizosaJanis K Burkhardt
May 18, 1999·Biochemical and Biophysical Research Communications·E A HodsonJ S Lymn
Sep 1, 1997·Archives of Biochemistry and Biophysics·Z PeiJ R Williamson
Feb 27, 2004·Biochemical and Biophysical Research Communications·Avishay Pelah, Meir Shinitzky

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