Linear motifs regulating protein secretion, sorting and autophagy in Leishmania parasites are diverged with respect to their host equivalents
Fig 2
A: Comparison of the sequence logos of all known or predicted KDEL-like motifs of five eukaryotes from different lineages show its conservation. B: This original K/H/RDEL consensus is altered in kinetoplastids, mostly yielding peptides ending in DL. C: Superimposed protein models show that the gatekeeper loop of the ER retrieval receptor (KDEL receptor) of kinetoplastids differs from other eukaryotes, clashing with the main chain of an incoming, canonical KDEL peptide (pdb:6I6H) in case of all examined parasitic species, but not in the free-living Bodo saltans. D: HADDOCK models show that the long gatekeeper loop forces the ligands of the Leishmania receptor to take a different main chain conformation than in the mammalian KDEL receptor. E: Recognizing the altered consensus of receptors allows the identification of conserved families of kinetoplastid ER-resident proteins including newly-identified protein groups (Blue bars show the presence of KDEL-like peptide-containing orthologs, while light blue bars indicate homologous proteins without KDEL).