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.
Original language | English |
---|---|
Pages (from-to) | 267-71 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 569 |
Issue number | 1-3 |
DOIs | |
Publication status | Published - 2 Jul 2004 |
MoE publication type | A1 Journal article-refereed |
Keywords
- Animals
- Cell Line
- Cell Membrane/physiology
- Cloning, Molecular
- Glial Cell Line-Derived Neurotrophic Factor
- Glial Cell Line-Derived Neurotrophic Factor Receptors
- Humans
- Membrane Glycoproteins/genetics
- Membrane Microdomains/metabolism
- Mice
- Nerve Growth Factors/metabolism
- Nerve Tissue Proteins/metabolism
- Neurites/physiology
- Neurons/cytology
- Proto-Oncogene Proteins/genetics
- Proto-Oncogene Proteins c-ret
- Rats
- Receptor Protein-Tyrosine Kinases/genetics
- Receptors, Nerve Growth Factor/genetics
- Recombinant Proteins/metabolism
- Transfection