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Title: Wnt3 Is Lipidated at Conserved Cysteine and Serine Residues in Zebrafish Neural Tissue
Authors: Dhasmana, Divya
Veerapathiran, Sapthaswaran 
Azbazdar, Yagmur
Nelanuthala, Ashwin Venkata Subba
Teh, Cathleen 
Ozhan, Gunes
Wohland, Thorsten 
Keywords: FCS diffusion law
fluorescence correlation spectroscopy
fluorescence cross-correlation spectroscopy
selective plane illumination microscopy
Issue Date: 26-May-2021
Publisher: Frontiers Media S.A.
Citation: Dhasmana, Divya, Veerapathiran, Sapthaswaran, Azbazdar, Yagmur, Nelanuthala, Ashwin Venkata Subba, Teh, Cathleen, Ozhan, Gunes, Wohland, Thorsten (2021-05-26). Wnt3 Is Lipidated at Conserved Cysteine and Serine Residues in Zebrafish Neural Tissue. Frontiers in Cell and Developmental Biology 9 : 671218. ScholarBank@NUS Repository.
Rights: Attribution 4.0 International
Abstract: Wnt proteins are a family of hydrophobic cysteine-rich secreted glycoproteins that regulate a gamut of physiological processes involved in embryonic development and tissue homeostasis. Wnt ligands are post-translationally lipidated in the endoplasmic reticulum (ER), a step essential for its membrane targeting, association with lipid domains, secretion and interaction with receptors. However, at which residue(s) Wnts are lipidated remains an open question. Initially it was proposed that Wnts are lipid-modified at their conserved cysteine and serine residues (C77 and S209 in mWnt3a), and mutations in either residue impedes its secretion and activity. Conversely, some studies suggested that serine is the only lipidated residue in Wnts, and substitution of serine with alanine leads to retention of Wnts in the ER. In this work, we investigate whether in zebrafish neural tissues Wnt3 is lipidated at one or both conserved residues. To this end, we substitute the homologous cysteine and serine residues of zebrafish Wnt3 with alanine (C80A and S212A) and investigate their influence on Wnt3 membrane organization, secretion, interaction and signaling activity. Collectively, our results indicate that Wnt3 is lipid modified at its C80 and S212 residues. Further, we find that lipid addition at either C80 or S212 is sufficient for its secretion and membrane organization, while the lipid modification at S212 is indispensable for receptor interaction and signaling. © Copyright © 2021 Dhasmana, Veerapathiran, Azbazdar, Nelanuthala, Teh, Ozhan and Wohland.
Source Title: Frontiers in Cell and Developmental Biology
ISSN: 2296-634X
DOI: 10.3389/fcell.2021.671218
Rights: Attribution 4.0 International
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