Structural basis for Mob1-dependent activation of the core Mst–Lats kinase cascade in Hippo signaling

Ni, Lisheng; Zheng, Yonggang; Hara, Mayuko; Pan, Duojia; Luo, Xuelian

doi:10.1101/gad.264929.115

Structural basis for Mob1-dependent activation of the core Mst–Lats kinase cascade in Hippo signaling

Journal Article · Wed Jun 24 00:00:00 EDT 2015 · Genes & Development

DOI:https://doi.org/10.1101/gad.264929.115· OSTI ID:1213722

Ni, Lisheng ^[1]; Zheng, Yonggang ^[2]; Hara, Mayuko ^[1]; Pan, Duojia ^[2]; Luo, Xuelian ^[1]

Univ. of Texas Southwestern Medical Center, Dallas, TX (United States). Dept. of Pharmacology
Johns Hopkins Univ., Baltimore, MD (United States). School of Medicine. Dept. of Molecular Biology and Genetics. Howard Hughes Medical Inst.

The Mst–Lats kinase cascade is central to the Hippo tumor-suppressive pathway that controls organ size and tissue homeostasis. The adaptor protein Mob1 promotes Lats activation by Mst, but the mechanism remains unknown. Here, we show that human Mob1 binds to autophosphorylated docking motifs in active Mst2. This binding enables Mob1 phosphorylation by Mst2. Phosphorylated Mob1 undergoes conformational activation and binds to Lats1. We determine the crystal structures of phospho-Mst2–Mob1 and phospho-Mob1–Lats1 complexes, revealing the structural basis of both phosphorylation-dependent binding events. Further biochemical and functional analyses demonstrate that Mob1 mediates Lats1 activation through dynamic scaffolding and allosteric mechanisms. Thus, Mob1 acts as a phosphorylation-regulated coupler of kinase activation by virtue of its ability to engage multiple ligands. We propose that stepwise, phosphorylation-triggered docking interactions of nonkinase elements enhance the specificity and robustness of kinase signaling cascades.

View Accepted Manuscript (DOE)

Research Organization:: Univ. of Texas Southwestern Medical Center, Dallas, TX (United States)

Sponsoring Organization:: National Inst. of Health (NIH) (United States); USDOE

Contributing Organization:: Johns Hopkins Univ., Baltimore, MD (United States)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1213722

Journal Information:: Genes & Development, Journal Name: Genes & Development Journal Issue: 13 Vol. 29; ISSN 0890-9369

Publisher:: Cold Springs Harbor Laboratory PressCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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59 BASIC BIOLOGICAL SCIENCES
Lats1
Mob1
Mst2
NMR
X-ray crystallography
autoinhibition
phosphorylation

Structural basis for Mob1-dependent activation of the core Mst–Lats kinase cascade in Hippo signaling

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References (53)

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