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. 2015 Jul 1;29(13):1416–1431. doi: 10.1101/gad.264929.115

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© 2015 Ni et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 5. — Phosphorylation-dependent conformational activation of Mob1. (A) Sequence alignment of the N-terminal region of Mob1. Secondary structural elements of pMob1 are drawn above the sequences. Secondary structural elements of S. cerevisiae (Sc) Mob1 are drawn below the sequences. The conserved FxFx₅KxF motif is colored magenta. T12 and T35 are colored red. (B) Superposition of ScMob1 (Protein Data Bank [PDB] code 2HJN) and pMob1–Lats1 structures (this study). Only the FxYx₅KxF motif-containing fragment from ScMob1 is shown. The Mob1-binding site of ScMob1 F112 is boxed. (C) Zoomed-in view of the boxed region in B to show that ScMob1 F112 (yellow sticks) and Lats1 R697 (gray sticks) occupy the same Mob1-binding site. (D) Model of phosphorylation-triggered conformational activation and Lats1 binding of Mob1. (E) Superposition of unphosphorylated Mob1^ΔN32 (PDB code 1PI1) and pMob1–Lats1 structures (this study). Mob1^ΔN32 is colored blue. The pMob1 core is colored green, and pMob1 NTE is colored orange. Lats1 is colored gray. The H0–H1 loop around pT35 is boxed. (F) Zoomed-in view of the boxed region in E to show the reorganization of the H0–H1 loop in pMob1 by T35 phosphorylation. Residues of Mob1^ΔN32 and pMob1 are shown as blue and orange sticks, respectively.