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The Adhesion GPCR GPR126 Has Distinct, Domain-Dependent Functions in Schwann Cell Development Mediated by Interaction with Laminin-211

Authors
Petersen Sarah C.Luo RongLiebscher InesGiera StefanieJeong Sung-JinMogha AmitGhidinelli MonicaFeltri M. LauraSchoeneberg TorstenPiao XianhuaMonk Kelly R.
Issue Date
Feb-2015
Publisher
CELL PRESS
Citation
NEURON, v.85, no.4, pp.755 - 769
Journal Title
NEURON
Volume
85
Number
4
Start Page
755
End Page
769
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/881
ISSN
0896-6273
Abstract
Myelin ensheathes axons to allow rapid propagation of action potentials and proper nervous system function. In the peripheral nervous system, Schwann cells (SCs) radially sort axons into a 1: 1 relationship before wrapping an axonal segment to form myelin. SC myelination requires the adhesion G protein-coupled receptor GPR126, which undergoes autoproteolytic cleavage into an N-terminal fragment (NTF) and a seven-transmembrane-containing C-terminal fragment (CTF). Here we show that GPR126 has domain-specific functions in SC development whereby the NTF is necessary and sufficient for axon sorting, whereas the CTF promotes wrapping through cAMP elevation. These biphasic roles of GPR126 are governed by interactions with Laminin-211, which we define as a novel ligand for GPR126 that modulates receptor signaling via a tethered agonist. Our work suggests a model in which Laminin-211 mediates GPR126-induced cAMP levels to control early and late stages of SC development.
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연구본부 (뇌발달질환 연구그룹)
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