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Updated: Jan 16, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
The Immunoglobulin Domain of SISS-1/EGF is Required for its Function
Jesse G Jones1, Cheryl Van Buskirk1
1Biology, California State University, Northridge, Northridge, California, United States.
None:
Epidermal growth factor (EGF) signaling plays roles in development and physiology across the animal kingdom. In the nematode C. elegans , a single EGF receptor (EGFR) and two EGF family ligands have been characterized. LIN-3 /EGF is required for a variety of developmental processes as well as ovulation, and SISS-1 /EGF promotes a damage-responsive quiescent state known as stress-induced sleep. Like all EGF family ligands, SISS-1 and LIN-3 are produced as transmembrane proteins with an extracellular EGF-like domain, known for its function in receptor binding. The ectodomain of SISS-1 , but not of LIN-3 , also contains an Immunoglobulin-like (Ig) domain, putting it into a class of Ig-EGFs that includes Drosophila Vein and certain vertebrate Neuregulins. The function of the Ig domain within Ig-EGFs appears to vary. Here, we investigate the SISS-1 Ig domain and show that it is essential for stress-induced sleep.
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