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J Biol Chem, Vol. 274, Issue 30, 20885-20894, July 23, 1999
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From the Glial cell line-derived neurotrophic factor
(GDNF) has been shown to signal through a multicomponent receptor
complex consisting of the Ret receptor tyrosine kinase and a member of
the GFR Division of Molecular Neurobiology,
Department of Neuroscience, Karolinska Institute, 17177 Stockholm,
Sweden and the ¶ Department of Neurological Surgery, University of
Louisville, Lousiville, Kentucky 40202
family of glycosylphosphatidylinositol-anchored receptors.
In the current model of GDNF signaling, Ret delivers the intracellular
signal but cannot bind ligand on its own, while GFRs bind ligand but are thought not to signal in the absence of Ret. We have compared signaling pathways activated by GDNF in two neuronal cell lines expressing different complements of GDNF receptors. In a
motorneuron-derived cell line expressing Ret and GFRs, GDNF
stimulated sustained activation of the Ras/ERK and phosphatidylinositol
3-kinase/Akt pathways, cAMP response element-binding protein
phosphorylation, and increased c-fos expression.
Unexpectedly, GDNF also promoted biochemical and biological responses
in a line of conditionally immortalized neuronal precursors that
express high levels of GFRs but not Ret. GDNF treatment did not
activate the Ras/ERK pathway in these cells, but stimulated a
GFR1-associated Src-like kinase activity in detergent-insoluble
membrane compartments, rapid phosphorylation of cAMP response
element-binding protein, up-regulation of c-fos mRNA,
and cell survival. Together, these results offer new insights into the
dynamics of GDNF signaling in neuronal cells, and indicate the
existence of novel signaling mechanisms directly or indirectly mediated
by GFR receptors acting in a cell-autonomous manner independently of Ret.
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