PUBLICATION

The Sec14-like phosphatidylinositol transfer proteins Sec14l3/SEC14L2 act as GTPase proteins to mediate Wnt/Ca2+ signaling.

Authors
Gong, B., Shen, W., Xiao, W., Meng, Y., Meng, A., Jia, S.
ID
ZDB-PUB-170504-14
Date
2017
Source
eLIFE   6: (Journal)
Registered Authors
Gong, Bo, Jia, Shunji, Meng, Anming
Keywords
cell biology, developmental biology, stem cells, zebrafish
MeSH Terms
  • Animals
  • Calcium Signaling*
  • Carrier Proteins/metabolism*
  • Cell Line
  • Frizzled Receptors/metabolism
  • GTP Phosphohydrolases/metabolism*
  • Humans
  • Lipoproteins/metabolism*
  • Phospholipid Transfer Proteins/metabolism*
  • Trans-Activators/metabolism*
  • Type C Phospholipases/metabolism
  • Wnt Signaling Pathway*
  • Zebrafish
PubMed
28463110 Full text @ Elife
Abstract
The non-canonical Wnt/Ca2+ signaling pathway plays important roles in embryonic development, tissue formation and diseases. However, it is unclear how the Wnt ligand-stimulated, G protein-coupled receptor Frizzled activates phospholipases for calcium release. Here, we report that the zebrafish/human phosphatidylinositol transfer protein Sec14l3/SEC14L2 act as GTPase proteins to transduce Wnt signals from Frizzled to phospholipase C (PLC). Depletion of sec14l3 attenuates Wnt/Ca2+ responsive activity and causes convergent and extension (CE) defects in zebrafish embryos. Biochemical analyses in mammalian cells indicate that Sec14l3-GDP forms complex with Frizzled and Dishevelled; Wnt ligand binding of Frizzled induces translocation of Sec14l3 to the plasma membrane; and then Sec14l3-GTP binds to and activates phospholipase Cδ4a (Plcδ4a); subsequently, Plcδ4a initiates phosphatidylinositol-4,5-bisphosphate (PIP2) signaling, ultimately stimulating calcium release. Furthermore, Plcδ4a can act as a GTPase-activating protein to accelerate the hydrolysis of Sec14l3-bound GTP to GDP. Our data provide a new insight into GTPase protein-coupled Wnt/Ca2+ signaling transduction.
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