The authors noticed an error in the Figure 2 legend. In the text, Ca+2 should read Ca2+. The authors have provided a corrected version here.
(A) In wild-type zebrafish (left), PrP-1 promotes proper delivery of E-cadherin from the Golgi to the plasma membrane (PM), possibly via activation of a signal transduction cascade involving Src-family tyrosine kinases. In morphant fish lacking PrP-1 (right), E-cadherin accumulates in intracellular vesicles, resulting in reduced delivery to the plasma membrane. As a result, Ca2+-dependent, cadherin-mediated cell adhesion is impaired. (B) PrP molecules on adjacent cells undergo homophilic interactions that promote cell adhesion in a Ca2+-independent manner, at the same time generating an intracellular signal involving tyrosine phosphorylation. The PrP functions depicted in the two panels of this figure could be linked, if the intracellular signal generated by homophilic binding of PrP molecules (B) regulates cadherin trafficking (A).
Citation: The PLOS Biology Staff (2014) Correction: Fishing for Prion Protein Function. PLoS Biol 12(6): e1001902. doi:10.1371/journal.pbio.1001902
Published: June 13, 2014
Copyright: © 2014 The PLOS Biology Staff. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.