PSPN/GFRalpha4 has a significantly weaker capacity than GDNF/GFRalpha1 to recruit RET to rafts, but promotes neuronal survival and neurite outgrowth

FEBS Letters
Jianmin YangM Saarma

Abstract

Previously, it was shown that the recruitment of RET into lipid rafts by glial cell line-derived neurotrophic factor (GDNF)/GFRalpha1 is crucial for efficient signal transduction. Here, we show that the mouse GFRalpha4 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/mGFRalpha4 promotes neurite outgrowth in PC6-3 cells and survival of cerebellar granule neurons. As we show that also human PSPN/GFRalpha4 is unable to recruit RET into lipid rafts, we propose that the mammalian GFRalpha4 in this respect differs from GFRalpha1.

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Citations

Jan 6, 2011·Journal of Molecular Medicine : Official Organ of the Gesellschaft Deutscher Naturforscher Und Ärzte·Macarena Ruiz-FerrerSalud Borrego
Dec 24, 2013·Molecular Neurobiology·Sandro SonninoAlessandro Prinetti
Jan 15, 2008·Journal of Neuroscience Methods·Li-Ying Yu, Urmas Arumäe
Oct 16, 2007·Annals of Medicine·Pia Runeberg-Roos, Mart Saarma
Jan 13, 2006·Trends in Pharmacological Sciences·Ora Schueler-FurmanMichal Linial
Jul 20, 2006·Endocrine Reviews·Jan Willem B de GrootRobert M W Hofstra
Jul 30, 2020·Cell and Tissue Research·Pia Runeberg-Roos, Richard D Penn
Dec 22, 2004·The Biochemical Journal·Heidi VirtanenPia Runeberg-Roos
Jun 29, 2005·Cytokine & Growth Factor Reviews·Elena ArighiHannu Sariola

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