TY - JOUR
T1 - Gurken, a TGF-α-like protein involved in axis determination in Drosophila, directly binds to the EGF-receptor homolog Egfr
AU - Shmueli, Anat
AU - Cohen-Gazala, Orit
AU - Neuman-Silberberg, F. Shira
N1 - Funding Information:
We thank Professor N. Isakov for anti-Myc antibody, Professor D. Raveh for the pYES2 plasmid and strain BJ2169, Professor E. Livneh and Dr. Y. Shmer-Avni for two-hybrid positive controls, and Professor B. Shilo for the spi clone. We are grateful to Professor T. Schupbach for valuable comments on the manuscript. This work was supported by grants from the Israel Science Foundation (ISF) and the Israeli Cancer Research Foundation (ICRF).
PY - 2002/1/1
Y1 - 2002/1/1
N2 - The establishment of axial polarity in the Drosophila egg and embryo depends on intercellular communication between two cell types in the ovary, the germ-line, and the soma. The genes gurken and egfr encode two essential players of this communication pathway. Gurken protein, a TGF-α-like molecule, is expressed in the germline, while the EGF-receptor homolog, Egfr, is expressed in the somatic cells of the ovary. Using the yeast two-hybrid system we show here, for the first time, that Gurken protein directly binds to the extra-cellular domain of Egfr. This direct physical association requires the presence of an intact EGF motif within Gurken protein. Furthermore, we provide evidence that this characteristic motif may be sufficient for interaction with the receptor, at list in vitro. Our results firmly establish Gurken as the germline ligand of Drosophila Egfr.
AB - The establishment of axial polarity in the Drosophila egg and embryo depends on intercellular communication between two cell types in the ovary, the germ-line, and the soma. The genes gurken and egfr encode two essential players of this communication pathway. Gurken protein, a TGF-α-like molecule, is expressed in the germline, while the EGF-receptor homolog, Egfr, is expressed in the somatic cells of the ovary. Using the yeast two-hybrid system we show here, for the first time, that Gurken protein directly binds to the extra-cellular domain of Egfr. This direct physical association requires the presence of an intact EGF motif within Gurken protein. Furthermore, we provide evidence that this characteristic motif may be sufficient for interaction with the receptor, at list in vitro. Our results firmly establish Gurken as the germline ligand of Drosophila Egfr.
KW - Drosophila
KW - EGF repeat
KW - Egfr
KW - Gurken
KW - TGF-α
KW - Two-hybrid
UR - http://www.scopus.com/inward/record.url?scp=0036296420&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2002.6426
DO - 10.1006/bbrc.2002.6426
M3 - Article
AN - SCOPUS:0036296420
SN - 0006-291X
VL - 291
SP - 732
EP - 737
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -