PUBLICATION
The Cys-His-Gly triplet within the WNT motif is essential for Wnt16 function in vivo
- Authors
- Ramirez, E.G., Rojas, M.F., Rai, J., Tang, W.J., Watson, C.J., Kwon, R.Y.
- ID
- ZDB-PUB-250828-4
- Date
- 2025
- Source
- microPublication. Biology 2025: (Journal)
- Registered Authors
- Watson, Claire
- Keywords
- none
- MeSH Terms
- none
- PubMed
- 40861003 Full text @ MicroPubl Biol
Citation
Ramirez, E.G., Rojas, M.F., Rai, J., Tang, W.J., Watson, C.J., Kwon, R.Y. (2025) The Cys-His-Gly triplet within the WNT motif is essential for Wnt16 function in vivo. microPublication. Biology. 2025:.
Abstract
WNTs are critical to many developmental and disease processes. They are post-translationally acylated at a serine within a highly conserved sequence termed the "WNT motif". Changes in individual amino acids in the WNT motif reduce but do not eliminate WNT function. However, the role of a highly conserved triplet of residues (Cys-His-Gly) upstream of the serine has yet to be examined. We show that an in-frame deletion of the Cys-His-Gly triplet in zebrafish Wnt16 likely functions as a null mutation. These findings highlight the utility of using small in-frame indels that target conserved amino acid regions to modulate protein function.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping