TY - JOUR
T1 - The bride of sevenless and sevenless interaction
T2 - Internalization of a transmembrane ligand
AU - Cagan, Ross L.
AU - Krämer, Helmut
AU - Hart, Anne C.
AU - Zipursky, S. Lawrence
N1 - Funding Information:
We would like to acknowledge the members of the Zipursky laboratory for helpful discussions. We also wish to thank E. Hafen for the anti-sev antibodies and the sev”Bfzz42 fly stock and M. Simon and G. Rubin for the SL2-sevcell line. This research is supported by the Howard Hughes Medical Institute and the following grants: a National institutes of Health Postdoctoral Fellowship (R. L. C.), an American Cancer Society Fellowship (H. K.), a US Public Health Service National Research Service Award (GM-07104; A. C. H.), a McKnight Foundation Development Award (S. L. Z.), and an NIH Grant. S. L. Z. is an Investigator of the Howard Hughes Medical Institute.
PY - 1992/5/1
Y1 - 1992/5/1
N2 - During Drosophila retinal development, the R8 photoreceptor neuron induces a neighboring cell to assume an R7 cell fate through cell contact. This is mediated by the transmembrane protein bride of sevenless (boss) on the surface of the R8 cell, which binds the sevenless tyrosine kinase receptor (sev) on the surface of the R7 precursor cell. The boss protein, which contains a large extracellular domain, seven transmembrane segments, and a C-terminal cytoplasmic domain, has an exceptional structure for a ligand of a receptor tyrosine kinase. Using a panel of antibodies directed to various cytoplasmic and extracellular epitopes, we demonstrate that the entire boss protein from its extreme N-terminus to its extreme C-terminus is internalized by sev-expressing tissue culture cells and by the R7 precursor cell in the developing eye imaginal disc. The receptor-mediated transfer of a transmembrane ligand represents a novel mechanism for protein transfer between developing cells.
AB - During Drosophila retinal development, the R8 photoreceptor neuron induces a neighboring cell to assume an R7 cell fate through cell contact. This is mediated by the transmembrane protein bride of sevenless (boss) on the surface of the R8 cell, which binds the sevenless tyrosine kinase receptor (sev) on the surface of the R7 precursor cell. The boss protein, which contains a large extracellular domain, seven transmembrane segments, and a C-terminal cytoplasmic domain, has an exceptional structure for a ligand of a receptor tyrosine kinase. Using a panel of antibodies directed to various cytoplasmic and extracellular epitopes, we demonstrate that the entire boss protein from its extreme N-terminus to its extreme C-terminus is internalized by sev-expressing tissue culture cells and by the R7 precursor cell in the developing eye imaginal disc. The receptor-mediated transfer of a transmembrane ligand represents a novel mechanism for protein transfer between developing cells.
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U2 - 10.1016/0092-8674(92)90442-F
DO - 10.1016/0092-8674(92)90442-F
M3 - Article
C2 - 1316239
AN - SCOPUS:0026632816
SN - 0092-8674
VL - 69
SP - 393
EP - 399
JO - Cell
JF - Cell
IS - 3
ER -