Fig. 5
From: Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation
Working hypothesis for hCPEB3 structural changes during memory consolidation. A The first 250 residues of hCPEB3 contain 4 α-helices (blue spirals); the first and third α-helices are relatively stable. Proline-rich segments (green) and SUMOylation as predicted to occur at K46 by in silico methods [24] prevent premature association and amyloid formation by the Q4RQ4 segment (magenta) and the hydrophobic motif (black squiggle). B Following deSUMOlyation and putatively phosphorylation, association between the fourth and first helices could occur, strengthened by hydrophobic and cation-π interactions. The Q4RQ4 segment may adopt an α-helix and associate with the Ala rich α-helices to form a coiled-coil. The structural transformations may well enhance intermolecular contacts within the dendritic P-body like granule, leading to gelification and, eventually, amyloid formation. C The final amyloid could be composed of the Q4RQ4 segment and hydrophobic tract and possibly the Ala-rich segments. The final configuration of the polyPro segments (green) may promote profilin binding and the initiation of a more robust actin filament network