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The adhesion GPCR GPR126 has distinct, domain-dependent functions in Schwann cell development mediated by interaction with laminin-211.

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.

journal_name

Neuron

journal_title

Neuron

authors

Petersen SC,Luo R,Liebscher I,Giera S,Jeong SJ,Mogha A,Ghidinelli M,Feltri ML,Schöneberg T,Piao X,Monk KR

doi

10.1016/j.neuron.2014.12.057

subject

Has Abstract

pub_date

2015-02-18 00:00:00

pages

755-69

issue

4

eissn

0896-6273

issn

1097-4199

pii

S0896-6273(14)01166-0

journal_volume

85

pub_type

杂志文章

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