1. A 4-midable Connection: CCR7 Tetramers Link GPCR to Src Kinase Signaling 
Reinhold Förster, Tim Worbs, Kathrin Werth 
Immunity 
Volume 44, Issue 1, Pages 9-11 (January 2016)
DOI: /j.immuni
Copyright © 2016 Elsevier Inc. Terms and Conditions

2. Figure 1 Signaling through CCR7
Left: Upon ligand binding, guanosine diphosphate (GDP) gets exchanged by guanosine triphosphate (GTP) leading to the dissociation of the α-β-γ heterotrimeric G protein complex into a α-GTP and a β-γ subunit. These in turn activate several parallel cascades of downstream molecules including phospholipase C (PLC), phosphatidylinositol 3-kinase (PI3K), mitogen-activated protein kinase (MAPK), and protein kinase C (PKC) that, among others, activate second messengers such as inositol trisphosphate (IP3), diacylglycerol (DAG), and Ca2+ ions (Randolph et al., 2008). Independent of G protein signaling, G protein receptor kinases (GRKs) phosphorylate C-terminal residues, allowing β-arrestin (β-arr)-mediated receptor internalization (Randolph et al., 2008). Right: Inflammatory signals such as PGE2 provoke oligomerization of CCR7. These oligomers serve as scaffolds that integrate signaling through G proteins and Src kinase. Src tyrosine phosphorylates CCR7 which then serves as a docking site for SH2-domain bearing molecules such as phosphatase SHP2.
Immunity  , 9-11DOI: ( /j.immuni )
Copyright © 2016 Elsevier Inc. Terms and Conditions