作者: Simone Prömel , Marie Frickenhaus , Samantha Hughes , Lamia Mestek , David Staunton
DOI: 10.1016/J.CELREP.2012.06.015
关键词:
摘要: Summary Adhesion class G protein-coupled receptors (aGPCR) form the second largest group of seven-transmembrane-spanning (7TM) whose molecular layout and function differ from canonical 7TM receptors. Despite their essential roles in immunity, tumorigenesis, development, mechanisms aGPCR activation signal transduction have remained obscure to date. Here, we use a transgenic assay define protein domains required in vivo for activity prototypical LAT-1/Latrophilin Caenorhabditis elegans . We show that GPCR proteolytic site (GPS) motif, hallmark feature entire class, is LAT-1 signaling serving two different modes receptor. Surprisingly, neither mode requires cleavage but presence GPS, which relays interactions with at least partners. Our work thus uncovers versatile nature detail places GPS motif central position diverse protein-protein interactions.