Phospholipase C-gamma 1 binds to actin-cytoskeleton via its C-terminal SH2 domain in vitro.
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.
Pei
Z
Z
Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia 19104, USA.
Yang
L
L
Williamson
J R
JR
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003599:Cytoskeleton / Q000378:metabolism*; D004815:Epidermal Growth Factor / Q000494:pharmacology; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000378:metabolism; D008297:Male; D051379:Mice; D051966:Phospholipase C gamma; D019000:Phosphotyrosine / Q000378:metabolism; D011485:Protein Binding; D051381:Rats; D017207:Rats, Sprague-Dawley; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D010738:Type C Phospholipases / Q000378:metabolism*; D018909:src Homology Domains
D000199:Actins; D007527:Isoenzymes; D011993:Recombinant Fusion Proteins; D019000:Phosphotyrosine; D004815:Epidermal Growth Factor; D010738:Type C Phospholipases; D051966:Phospholipase C gamma