Fig. 1 | Nature Communications

Fig. 1

From: Hexameric NuMA:LGN structures promote multivalent interactions required for planar epithelial divisions

Fig. 1

LGN and NuMA engage into high-molecular weight oligomers. a Cartoon representation of LGN and NuMA domain structures. Bold lines with numbers indicate protein subdomains being used in the in vitro binding assays. b SEC elution profiles of LGNTPR (20 μM) in complex with NuMA1821–2001 (20 μM), NuMALGNBD (20 μM) or NuMAPEPT/NuMA1900–1928 (40 μM). The run of globular molecular weight markers is indicated in gray. The early elution volume of LGNTPR:NuMALGNBD indicates they form higher molecular species compared with the 1:1 stoichiometric LGNTPR:NuMAPEPT/NuMA1900–1928 dimer. Coomassie-stained SDS-PAGE in color-coded boxes show the protein composition of each elution profile. c Table of static light scattering (SLS) experiments conducted with the trimmed LGN:NuMA constructs used in Fig. 1b–d, and Supplementary Fig. 2a, b. SLS measurements shown in green indicate oligomerizing complexes, while red values belong to oligomerization-deficient LGN:NuMA pairs. d SEC analyses conducted with LGNTPR truncations and NuMALGNBD. The oligomerization determinants span residues 1–12 and 351–409 on LGN. e SLS analysis indicating that the LGN7–367 and NuMALGNBD engage in 142.5 kDa oligomers compatible with a 3:3 stoichiometry. This also suggests that LGN7–367 is the minimal oligomerization domain of LGN

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