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GDE2 Promotes Neurogenesis by Glycosylphosphatidylinositol-Anchor Cleavage of RECK
- Source :
- Science. 339:324-328
- Publication Year :
- 2013
- Publisher :
- American Association for the Advancement of Science (AAAS), 2013.
-
Abstract
- Signaling Differentiation The six-transmembrane protein GDE2 promotes differentiation through extracellular glycerophosphodiester phosphodiesterase (GDPD) activity and induces neuronal differentiation through inhibition of Notch signaling—a major pathway that maintains stem or progenitor cell states and is implicated in multiple cancers. How then, does GDPD activity inhibit Notch signaling, given that GDPD enzymes are known to metabolize glycerophosphodiesters into glycerol-3-phosphate and corresponding alcohols? Park et al. (p. 324 ) show that the six-transmembrane GDPDs such as GDE2, do not function as conventional GDPD enzymes, but instead cleave the glycosylphosphatidylinositol (GPI) anchors of GPI-anchored proteins. GDE2 GDPD activity cleaves and inactivates the GPI-anchored protein RECK, which normally acts to prevent shedding of the Notch ligand Delta. Accordingly, RECK inactivation stimulates Delta shedding leading to Notch inactivation in progenitors and the initiation of cellular differentiation.
- Subjects :
- Glycosylphosphatidylinositols
Neurogenesis
Notch signaling pathway
Chick Embryo
GPI-Linked Proteins
Kazal Motifs
Article
Disintegrin
Animals
RNA, Small Interfering
Motor Neurons
Glycerophosphodiester phosphodiesterase
Multidisciplinary
Receptors, Notch
biology
Phosphoric Diester Hydrolases
Activator (genetics)
Phosphodiesterase
ADAM Proteins
Cell biology
Spinal Cord
Biochemistry
biology.protein
Intercellular Signaling Peptides and Proteins
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 339
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....d7c00907ec3cae76ecff798e2962449a