EXTRACELLULAR DOMAIN OF THE BOSS TRANSMEMBRANE LIGAND ACTS AS AN ANTAGONIST OF THE SEV RECEPTOR

被引:38
作者
HART, AC [1 ]
KRAMER, H [1 ]
ZIPURSKY, SL [1 ]
机构
[1] UNIV CALIF LOS ANGELES,INST MOLEC BIOL,DEPT BIOL CHEM,HOWARD HUGHES MED INST,LOS ANGELES,CA 90024
关键词
D O I
10.1038/361732a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 [理学]; 0710 [生物学]; 09 [农学];
摘要
THE fate of the R7 photoreceptor cell in the Drosophila compound eye is established by a specific inductive interaction between the R8 photoreceptor neuron and the R7 precursor cell1. This induction is mediated by two cell-surface proteins: the ligand, bride of sevenless2 (boss), and sevenless (sev), a tyrosine-kinase receptor3-5 The structure of boss is unique for a ligand of a tyrosine-kinase receptor. It contains a large extracellular domain, seven transmembrane segments, and a carboxy-terminal cytoplasmic tail6,7. Here we report that: (1) boss activates tyrosine phosphorylation of the sev receptor; (2) the seven transmembrane domain of boss is necessary for its function; and (3) a soluble form of boss acts as an antagonist of the sev receptor both in vivo and in vitro.
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页码:732 / 736
页数:5
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