Structural highlights
Function
7LESS_DROME Receptor for an extracellular signal required to instruct a cell to differentiate into an R7 photoreceptor. The ligand for sev is the boss (bride of sevenless) protein on the surface of the neighboring R8 cell.[1]
Publication Abstract from PubMed
Sevenless (Sev) is a Drosophila receptor tyrosine kinase (RTK) required for the specification of the R7 photoreceptor. It is cleaved into alpha and beta subunits and binds the ectodomain of the G-protein-coupled receptor bride of sevenless (Boss). Previous work showed that the Boss ectodomain could bind but not activate Sev; rather, the whole seven-pass transmembrane Boss was required. Here, we show that Sev does not need to be cleaved to function and that a single-pass transmembrane form of Boss activates Sev. We use cryo-electron microscopy and biophysical methods to determine the structural basis of ligand binding and pH-dependent dimerization of Sev, and we discuss the implications in the process of Sev activation. The Sev human homolog, receptor oncogene from sarcoma 1 (ROS1), is associated with oncogenic transformations, and we discuss their structural similarities.
, PMID:39510067[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Basler K, Hafen E. Control of photoreceptor cell fate by the sevenless protein requires a functional tyrosine kinase domain. Cell. 1988 Jul 29;54(3):299-311. PMID:2840202 doi:10.1016/0092-8674(88)90193-6
- ↑ Cerutti G, Arias R, Bahna F, Mannepalli S, Katsamba PS, Ahlsen G, Kloss B, Bruni R, Tomlinson A, Shapiro L. Structures and pH-dependent dimerization of the sevenless receptor tyrosine kinase. Mol Cell. 2024 Dec 5;84(23):4677-4690.e6. PMID:39510067 doi:10.1016/j.molcel.2024.10.017
