title: Splicing and proteolytic processing in VEGF signaling: now it is the coreceptor's turn.
abstract: Alternative splicing and proteolytic processing of VEGFs generate proteins with distinct physiological roles. In this issue of Structure, Parker et al. show that proteolysis of an isoform of the VEGF-C coreceptor Nrp2 produces a soluble receptor that inhibits VEGF-C/Nrp2 interactions.
authors: Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
authors: Xiaolan
authors: X
authors: Yao
authors: Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110, USA; Department of Neurology and Cognitive Sciences, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA. Electronic address: bouyains@umkc.edu.
authors: Samuel
authors: S
authors: Bouyain
mesh_terms: D006801:Humans; D039943:Neuropilin-2 / Q000737:chemistry*; D042582:Vascular Endothelial Growth Factor C / Q000737:chemistry*
chemical_list: D039943:Neuropilin-2; D042582:Vascular Endothelial Growth Factor C