Abstract
Association of phospholipase C (PLC)-γ1 with the cytoskeleton has been postulated to be one of the crucial steps for PLC-γ1 activation and translocation to the plasma membrane. In this report, direct binding assays were carried out to study which fragment of PLC-γ1 Src-homology region has been able to bind to the actin-cytoskeleton. Using GST fusion proteins containing various deletions of the PLC-γ1 Src homology region, it was found that PLC-γ1 binds to the actin-cytoskeleton directly via its C-terminal SH2 domain but not the SH3 domainin vitro.However, the binding of the C-terminal SH2 domain of PLC-γ1 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-γ1.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
