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. Author manuscript; available in PMC: 2020 Apr 30.
Published in final edited form as: Cell Rep. 2020 Mar 2;30(11):3699–3709.e6. doi: 10.1016/j.celrep.2020.02.086

Figure 4. Ric-8A Phosphorylated Residues S435 and T440 Stabilize the R8-R9 ARM/HEAT Interaction with the Ras-like Domain Core.

Figure 4.

(A) Electrostatic surface representation of Ric-8A 1–421 (8 to +8 kT/e electrostatic potential is colored from red to blue respectively). Ric-8A residues 422–482 and Gαi1 are shown as ribbon models in blue and gold, respectively. Phosphorylated residues S435 and T440 are shown as spheres.

(B) Ribbon diagram of Ric-8A 1–482 (blue) and Gαi1 (gold) of the phosphorylated, full-length Ric-8A-Gαi1 complex. Phosphorylated residues S435 and T440 are shown as sticks.

(C) Phosphorylated residues S435 and T440 bind to conserved positively charged residues of Ric-8A.

(D) Sequence alignment of Ric-8 residues interacting with the phosphorylated S435 and T440 sites. The positively charged interacting residues (*) are highly conserved in both mammalian Ric-8 isoforms and across species.