Work

The Cys-His-Gly triplet within the WNT motif is essential for Wnt16 function in vivo

Year: 2025

Type: article

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.

Source: PubMed

DOI: 10.17912/micropub.biology.001736

Authors: Emily G. Ramirez, Maria F. Rojas, Jyoti Rai, W. Joyce Tang, Claire J. Watson, Ronald Young Kwon

Institution: University of Washington

Language: English

Topic: Wnt/β-catenin signaling in development and cancer

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of Arthritis and Musculoskeletal and Skin Diseases

Award: Causal Genes at BMD Loci