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PSPN/GFRα4 has a significantly weaker capacity than GDNF/GFRα1 to recruit RET to rafts, but promotes neuronal survival and neurite outgrowth
Author(s) -
Yang Jianmin,
Lindahl Maria,
Lindholm Päivi,
Virtanen Heidi,
Coffey Eleanor,
Runeberg-Roos Pia,
Saarma Mart
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.06.007
Subject(s) - glial cell line derived neurotrophic factor , lipid raft , neurite , microbiology and biotechnology , phosphorylation , gdnf family of ligands , neurotrophic factors , signal transduction , neurotrophin , biology , chemistry , receptor , biochemistry , in vitro
Previously, it was shown that the recruitment of RET into lipid rafts by glial cell line‐derived neurotrophic factor (GDNF)/GFRα1 is crucial for efficient signal transduction. Here, we show that the mouse GFRα4 is a functional, N ‐glycosylated, glycosylphosphatidylinositol (GPI)‐anchored protein, which mediates persephin (PSPN)‐induced phosphorylation of RET, but has an almost undetectable capacity to recruit RET into the 0.1% Triton X‐100 insoluble membrane fraction. In spite of this, PSPN/mGFRα4 promotes neurite outgrowth in PC6‐3 cells and survival of cerebellar granule neurons. As we show that also human PSPN/GFRα4 is unable to recruit RET into lipid rafts, we propose that the mammalian GFRα4 in this respect differs from GFRα1.