Domain architecture, post-translation modification and binding/functional regions of NDE1 and NDEL1.
Schematics of NDE1 (top panel) and NDEL1 (bottom panel) drawn to scale depicting the N-terminal coiled-coil domain and the predicted C-terminal α-helix (labeled); the central flexible linker region connects these two structured regions, while another unstructured region lies at the extreme C-terminus of the proteins. Numerous PTMs (stars) reside within delineated protein-protein interaction sites, sub-cellular localization regions, or oligomerization domains with the vast majority located within predicted unstructured regions of the proteins. Minimal essential protein-binding sites from the literature are shown drawn to scale (NDE1: green bars; NDEL1: purple bars). References for each NDE1 interaction site are as follows: Centrosomal targeting (98); Centromere protein F (CENPF)/Mitosin/LEK1 (112); LIS1 (4); Utrophin (66); MCRS1/p78 (99); Su48/ DBZ/ZNF365 (98); Dynein IC (89); Dynein (LC8) (49). References for each NDEL1 interaction site are as follows: Centrosomal targeting (113); LIS1 (96); Dynamitin (50); Pericentrin/Kendrin (113); Paxillin (114); G-protein β (Gβ) (115); DISC1 (28); Katanin p60 and p80 (68); 14-3-3ε (100); Neurofilament (NF)-L (72); Dynamin-2 (75); Rabaptin-5 (78); Dynein intermediate chain (IC) (89); Dynein heavy chain (HC) (1); Cdc42GAP (74); Lamin-B (63). Note: the palmitoylation site C273 (red star) on NDEL1 is also the site of endooligopeptidase activity (77). In the majority of cases, these sites have only been investigated for one of NDE1 or NDEL1; it is likely that some of them will be conserved between the two proteins. The effect of PTMs should be tested on protein conformation, stability, oligomerization, modulation of protein-protein interaction and cellular trafficking/targeting.