The SH2-SH2-SH3 domain of phospholipase C-gamma1 directly binds to translational elongation factor-1alpha.
Phospholipase C-gamma1 (PLC-gamma1) is a lipase that hydrolyzes PIP2 to generate two second messengers, IP3 and DAG. By using the yeast two-hybrid system, we identified the translational elongation factor-1alpha (EF-1alpha) as a binding protein of PLC-gamma1 from the human B-lymphocyte library. Direct interaction between EF-1alpha and PLC-gamma1 was confirmed by the in vitro binding experiment using purified PLC-gamma1. Furthermore, from the in vitro binding experiment, we could demonstrate that the carboxyl terminal region of EF-1alpha is involved in the interaction with PLC-gamma1, and that both SH2 and SH3 domains of PLC-gamma1 are required for the interaction with EF-1alpha. In vivo interaction between EF-1alpha and PLC-gamma1 was confirmed by the immunoprecipitation experiment using anti-EF-1alpha antibody. The interaction between EF-1alpha and PLC-gamma1 was enhanced by EGF-treatment. Taken together, we suggest that EF-1alpha might play a role in PLC-gamma1-mediated signal transduction.
Kim
M J
MJ
Department of Life Science and School of Environmental Engineering, Pohang University of Science and Technology, Korea.
Si
F
F
Kim
S J
SJ
Hong
S B
SB
Hwang
J I
JI
Lee
H J
HJ
Lee
S J
SJ
Chang
J S
JS
Lee
Y H
YH
Ryu
S H
SH
Suh
P G
PG
D000818:Animals; D019556:COS Cells; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D008214:Lymphocytes / Q000378:metabolism; D020648:Peptide Elongation Factor 1 / Q000378:metabolism*; D051966:Phospholipase C gamma; D011233:Precipitin Tests; D011485:Protein Binding; D015398:Signal Transduction; D014162:Transfection; D010738:Type C Phospholipases / Q000378:metabolism*; D015003:Yeasts; D018909:src Homology Domains
D007527:Isoenzymes; D020648:Peptide Elongation Factor 1; D010738:Type C Phospholipases; D051966:Phospholipase C gamma