Schematic model of ERp44 regulation.

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Schematic model of ERp44 regulation. Schematic model of ERp44 regulation. The lower pH encountered by ERp44 as it proceeds along the early secretory pathway, favors opening of the C-tail and KDELR binding regardless of the presence or absence of high-affinity client proteins. Accordingly, ERp44 mutants that bind few, if any, substrates in cells (e.g. ERp44C29S; Anelli et al., 2003) are not secreted. By contrast, mutants lacking key conserved histidine residues or a loop at the border between the domain-b′ and the tail (star) bind poorly to KDELRs, proceed towards the extracellular space and are O-glycosylated. Client binding induces KDELR-dependent retrieval of histidine mutants before (Ero1, Prx4) or after (Sumf1) O-glycosylation takes place. Given that histidine mutants remain pH sensitive in vitro, we hypothesize that histidine-region binding factor(s) (HRBF) favor tail movements in vivo, allowing efficient RDEL exposure. Sara Sannino et al. J Cell Sci 2014;127:4260-4269 © 2014. Published by The Company of Biologists Ltd