Correction: Raasakka, A.; Kursula, P. Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease. Cells 2020, 9, 470

The authors would like to make corrections to their review [...].

The authors would like to make corrections to their review [1] in the light of two recently retracted papers [2,3]. These papers (citations 202 and 203 in the original publication) were cited and the information within was discussed in our review, as well as used in the preparation of Figure 8. We have now removed these citations and all information from the two retracted papers by modifying our review text, as described below.
The following text from Section 2.7 has been updated by replacing citation 202 with citation 200: "The interaction is thought to be mainly mediated by the DRP2 spectrin repeat domain, with possible involvement of the adjacent WW domain and NLS2/NLS3 in L-PRX ( Figure 8b) [13,202]".
The following text from Section 2.7 has been deleted: "The NLS2/NLS3 region mediates a self-interaction within L-PRX by binding to the L-PRX acidic C terminus, although it is unclear whether the interaction is intramolecular or if two L-PRX molecules may interact [203]".
The following text from Section 2.7 has been deleted: "The C-terminal acidic region is rich in Glu, which is believed to be the basis of the interaction with NLS2 and NLS3 of the basic region ( Figure 8b). The collective negative charge is likely to play a profound role in the association, although one specific point mutation, E1259K, had a significant inhibitory effect [203]".
The following text from the end of paragraph eight in Section 2.7 has been deleted: "(see below)".
The following text from Section 2.7 has been deleted: "Finally, the self-association of the acidic domain with the tripartite NLS might harbor similar roles in either nuclear export or inhibition of DRP2 and/or integrin β4 binding [203]. It remains to be determined, whether the mechanism involves two interacting L-PRX molecules or an intramolecular switch within a single L-PRX molecule that concurrently forms hetero-and homodimers via the PDZ domain".
The following paragraph in Section 2.7 has been deleted: "Bringing several L-PRX molecules together through the aforementioned interactions could result in large-scale assemblies that undergo liquid-liquid phase separation. This could harbor a regulatory role in the formation and stability of the periaxinosome, for instance through the controlled release of free L-PRX to the cytosol or to the membrane surface [216]. The binding of ezrin to L-PRX, or S-PRX heterodimerization with L-PRX, might function as a control mechanism for the formation of phase-separated compartments in the periaxinosome".
The following text from Section 3.2 has been deleted: "The only missense mutation that has a known effect is E1259K, which abolishes the internal L-PRX interaction [203]".
The following text from Section 4 "The intramolecular interaction within L-PRX and the potential regulatory role of S-and L-PRX heterodimerization need to be characterized at the molecular level, in order to shed light on PRX nuclear trafficking and the formation of the periaxinosome." has been modified to: "The potential regulatory role of S-and L-PRX heterodimerization needs to be characterized at the molecular level, in order to shed light on PRX nuclear trafficking and the formation of the periaxinosome". The following text from Section 4 "The intramolecular interaction within L-PRX and the potential regulatory role of S-and L-PRX heterodimerization need to be characterized at the molecular level, in order to shed light on PRX nuclear trafficking and the formation of the periaxinosome." has been modified to: "The potential regulatory role of S-and L-PRX heterodimerization needs to be characterized at the molecular level, in order to shed light on PRX nuclear trafficking and the formation of the periaxinosome." Figure 8 has been modified. The updated figure and figure legend are shown below. AnxA2 and S100A10 binding region, as reported earlier for AHNAK [195,196]. See Table 1 for mutation details. (b) L-PRX is an assembler within abaxonal non-compact myelin, linking dystroglycans and integrins together in membrane appositions, forming the periaxinosome. These interaction partners connect the Schwann cell basal lamina to the Schwann cell cytoplasm. S-PRX forms heterodimers with L-PRX, which might allow regulation of the cytoplasmic assembly as well as the nuclear export of L-PRX. Ezrin in complex with hetero-or homodimeric L-PRX might have relevance in such regulations, especially considering its phosphoregulated membrane-binding activity [197]. The function of the S-PRX homodimer is unknown. The significance of the putative L-PRX/AnxA2/Sl00A10 ternary complex could involve linking the entire assembly via AnxA2 and Ca 2+ to the underlying membrane, possibly forming a structural basis for membrane appositions that line Cajal bands in myelinating Schwann cells. Dashed boxes and lines denote protein-protein interactions. L-PRX contains a predicted AnxA2 and S100A10 binding region, as reported earlier for AHNAK [195,196]. See Table 1 for mutation details.
(b) L-PRX is an assembler within abaxonal non-compact myelin, linking dystroglycans and integrins together in membrane appositions, forming the periaxinosome. These interaction partners connect the Schwann cell basal lamina to the Schwann cell cytoplasm. S-PRX forms heterodimers with L-PRX, which might allow regulation of the cytoplasmic assembly as well as the nuclear export of L-PRX. Ezrin in complex with hetero-or homodimeric L-PRX might have relevance in such regulations, especially considering its phosphoregulated membrane-binding activity [197]. The function of the S-PRX homodimer is unknown. The significance of the putative L-PRX/AnxA2/Sl00A10 ternary complex could involve linking the entire assembly via AnxA2 and Ca 2+ to the underlying membrane, possibly forming a structural basis for membrane appositions that line Cajal bands in myelinating Schwann cells. The authors apologize for any inconvenience caused. The original article has been updated.