GDNF–Induced Activation of the Ret Protein Tyrosine Kinase Is Mediated by GDNFR-α, a Novel Receptor for GDNF

@article{Jing1996GDNFInducedAO,
  title={GDNF–Induced Activation of the Ret Protein Tyrosine Kinase Is Mediated by GDNFR-$\alpha$, a Novel Receptor for GDNF},
  author={Shuqian Jing and Duanzhi Wen and Yan Bin Yu and Paige Holst and Yi Luo and Mei Fang and Rami Tamir and Laarni Antonio and Zheng Hu and Rod L. Cupples and Jean Claude Louis and Sylvia Hu and Bruce W. Altrock and Gary M. Fox},
  journal={Cell},
  year={1996},
  volume={85},
  pages={1113-1124}
}
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Multiple GPI-Anchored Receptors Control GDNF-Dependent and Independent Activation of the c-Ret Receptor Tyrosine Kinase
TLDR
Combined roles for GFR alpha receptors in the regulation of c-Ret activity and the maintenance of distinct neuronal circuits in the central and peripheral nervous systems are indicated.
Glial cell line-derived neurotrophic factor-dependent RET activation can be mediated by two different cell-surface accessory proteins.
TLDR
The isolation and characterization of rat and human cDNAs for a novel cell-surface associated accessory protein, RETL2, that shares 49% identity with RETL1 are reported, raising the possibility that RETL 1 andRETL2 have distinctive roles during development and in the nervous system of the adult.
Internalization of Glial Cell-Derived Neurotrophic Factor Receptor GFRα1 in the Absence of the Ret Tyrosine Kinase Coreceptor
TLDR
The data suggest different mechanisms of internalization for GDNF–GFRα1 in the absence and presence of the Ret coreceptor, and indicates that this coreceptor tyrosine kinase slows internalization at early time points.
Ret-dependent and -independent Mechanisms of Glial Cell Line-derived Neurotrophic Factor Signaling in Neuronal Cells*
TLDR
Compared signaling pathways activated by GDNF in two neuronal cell lines expressing different complements of GDNF receptors are compared to indicate the existence of novel signaling mechanisms directly or indirectly mediated by GFRα receptors acting in a cell-autonomous manner independently of Ret.
Expression of GDNF Family Receptor Components during Development: Implications in the Mechanisms of Interaction
TLDR
There are multiple mechanisms regulating the interaction between Ret and the α-receptors that mediates the effects of GDNF family trophic factors on the survival and differentiation of cells and on neuron–target interactions in the nervous system.
Glial Cell Line-derived Neurotrophic Factor Induces Ret-mediated Lamellipodia Formation*
TLDR
It is shown that glial cell line-derived neurotrophic factor can serve as a genuine ligand for Ret and can induce Ret-mediated formation of lamellipodia, cell surface protrusions that are implicated in neuritogenesis.
Differential effects of glial cell line‐derived neurotrophic factor and neurturin in RET/GFRα1‐expressing cells
TLDR
The findings not only show the differential signaling of GDNF and neurturin but also suggest that this can be achieved through binding to the same GFRα subtype, leading to distinct biological responses.
Molecular Cloning and Expression Analysis of GFRα-3, a Novel cDNA Related to GDNFRα and NTNRα
TLDR
Results indicate that the tissue distribution of GFR alpha-3 mRNA is different from that of GDNFR alpha or NTNR alpha mRNA, and suggest that GFRalpha-3 may function in differentiation of embryonic cells expressing its mRNA.
c-Src Is Required for Glial Cell Line-Derived Neurotrophic Factor (GDNF) Family Ligand-Mediated Neuronal Survival via a Phosphatidylinositol-3 Kinase (PI-3K)-Dependent Pathway
TLDR
The data implicate Src as one of the major signaling molecules involved in GDNF-mediated bioactivity, and the importance of protein–protein interactions between Ret and raft-associated proteins in the signaling pathways elicited by GDNF is confirmed.
Zebrafish GDNF and its co-receptor GFRα1 activate the human RET receptor and promote the survival of dopaminergic neurons in vitro
TLDR
Zebrafish GDNF as well as zebrafish GFRα1 robustly activated human RET signaling and promoted the survival of cultured mouse dopaminergic neurons with comparable efficiency to mammalian GDNF, unlike E. coli-produced human proteins.
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