This article is a correction to:
WNT5B in Physiology and Disease
Sarocha Suthon
Rachel S. Perkins
Vitezslav Bryja
Gustavo A. Miranda-Carboni
Susan A. Krum- 1Department of Orthopaedic Surgery and Biomedical Engineering, University of Tennessee Health Science Center, Memphis, TN, United States
- 2Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czechia
- 3Department of Cytokinetics, Institute of Biophysics, Czech Academy of Sciences, Brno, Czechia
- 4Division of Hematology and Oncology, Department of Medicine, University of Tennessee Health Science Center, Memphis, TN, United States
- 5Center for Cancer Research, University of Tennessee Health Science Center, Memphis, TN, United States
A Corrigendum on
WNT5B in Physiology and Disease
by Suthon, S., Perkins, R. S., Bryja, V., Miranda-Carboni, G. A., and Krum, S. A. (2021). Front. Cell Dev. Biol. 9:667581. doi: 10.3389/fcell.2021.667581
In the original article, there were two errors.
(1) Our information on Wnt modification and secretion was out of date. Mouse Wnts are not palmitoleated on cysteines—that was an error in mutational analysis by Karl Willert. All the cysteines in Wnt are engaged in disulfide bonds (DOI 10.1126/science.1222879, 10.1074/jbc.m114.575027). However, a new reference describes WNT palmitoylation in zebrafish WNT3A (Dhasmana et al., 2021).
(2) The WLS protein binds to Wnt in the ER, not the Golgi. The Golgi localization of WLS was also an error due to the use of an epitope tag on the c-terminus (10.1016/j.devcel.2014.03.016, 10.1016/j.cell.2020.11.038).
A correction has been made to the introduction, paragraph number 2
The WNT family now contains 19 WNT genes, falling into 12 WNT subfamilies in mammalian genomes. All WNT genes encode proteins around 40 kDa in size and contain highly conserved cysteines (Miller, 2002; Clevers and Nusse, 2012). Mammalian WNT proteins are palmitoylated at conserved serine residues by a special palmitoyl transferase, Porcupine (PORCN), in the endoplasmic reticulum (Takada et al., 2006; Galli et al., 2007; Rios-Esteves et al., 2014). Zebrafish WNT3 is lipidated at both cysteine and serine residues (Dhasmana et al., 2021). The activity of PORCN is essential for the secretion of WNT ligands. Then, the seven-transmembrane protein Wntless/Evi (Wls) in the endoplasmic reticulum escorts mature hydrophobic WNT proteins to be secreted at the plasma membrane or released in exosomes, leading to both autocrine and paracrine effects (Banziger et al., 2006; Routledge and Scholpp, 2019).
Accordingly, the following reference has been added to the original article:
Dhasmana, D., Veerapathiran, S., Azbazdar, Y., Nelanuthala, A. V. S., Teh, C., Ozhan, G., et al. (2021). Wnt3 is lipidated at conserved cysteine and serine residues in zebrafish neural tissue. Front. Cell Dev. Biol. 9:671218. 10.3389/fcell.2021.671218
And the following reference has been removed from the original article:
Willert, K., Brown, J. D., Danenberg, E., Duncan, A. W., Weissman, I. L., Reya, T., et al. (2003). Wnt proteins are lipid-modified and can act as stem cell growth factors. Nature 423, 448–452.
The authors apologize for these errors and state that this does not change the scientific conclusions of the article in any way. The original article has5 been updated.
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References
Banziger, C., Soldini, D., Schutt, C., Zipperlen, P., Hausmann, G., and Basler, K. (2006). Wntless, a conserved membrane protein dedicated to the secretion of Wnt proteins from signaling cells. Cell. 125, 509–522. doi: 10.1016/j.cell.2006.02.049
Dhasmana, D., Veerapathiran, S., Azbazdar, Y., Nelanuthala, A. V. S., Teh, C., Ozhan, G., et al. (2021).Wnt3 is lipidated at conserved cysteine and serine residues in zebrafish neural tissue. Front. Cell Dev. Biol. 9:671218. doi: 10.3389/fcell.2021.671218
Galli, L. M., Barnes, T. L., Secrest, S. S., Kadowaki, T., and Burrus, L. W. (2007). Porcupine-mediated lipid-modification regulates the activity and distribution of Wnt proteins in the chick neural tube. Development. 134, 3339–3348. doi: 10.1242/dev.02881
Rios-Esteves, J., Haugen, B., and Resh, M. D. (2014). Identification of key residues and regions important for porcupine-mediated Wnt acylation. J. Biol. Chem. 289, 17009–17019. doi: 10.1074/jbc.m114.561209
Routledge, D., and Scholpp, S. (2019). Mechanisms of intercellular Wnt transport. Development. 146:dev176073. doi: 10.1242/dev.176073
Keywords: Wnt5B, Wnt signaling, development, cancer, Wnt5a
Citation: Suthon S, Perkins RS, Bryja V, Miranda-Carboni GA and Krum SA (2021) Corrigendum: WNT5B in Physiology and Disease. Front. Cell Dev. Biol. 9:724948. doi: 10.3389/fcell.2021.724948
Received: 14 June 2021; Accepted: 23 June 2021;
Published: 23 July 2021.
Edited and reviewed by: Gunes Ozhan, Dokuz Eylül University, Turkey
Copyright © 2021 Suthon, Perkins, Bryja, Miranda-Carboni and Krum. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Susan A. Krum, smirand5@uthsc.edu