Evidence map›Paper›PMID 26108669›Full record

ArticleGenes & development2015

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

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

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

99 citing papers in PubMed, 164 citations in OpenAlex.

  1. Article
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  3. Regulation of STK38 by autophagy governs YAP1 activity during paligenosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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39 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Lisheng NiDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA;
Yonggang ZhengHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Mayuko HaraDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA;
Duojia PanHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Xuelian LuoDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA;
The University of Texas Southwestern Medical Center · USJohns Hopkins University · US

Funding

Control of Cell Number in Developing RetinaR01EY015708 · NEI · UT SOUTHWESTERN MEDICAL CENTER · PI DUOJIA PAN · 2004 to 2026
$8.8M
Structure and Function of Spindle Checkpoint ProteinsR01GM085004 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LUO, XUELIAN · 2008 to 2012
$1.4M
Activation mechanism of the tumor-suppressing MST-LATS kinase cascadeR01GM107415 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LUO, XUELIAN · 2013 to 2016
$1.2M
600MHz Varian VNMRS Console UpgradeS10RR026461 · NCRR · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 2010 to 2010
$254k
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR026461NCRR NIH HHS S10RR026461-01NEI NIH HHS EY015708NEI NIH HHS R01 EY015708NIGMS NIH HHS GM085004NIGMS NIH HHS R01 GM085004NIGMS NIH HHS R01 GM107415
6 · The paper itself

Abstract

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.

Indexed as

Adaptor Proteins, Signal TransducingModels, MolecularSignal TransductionAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCells, CulturedCrystallizationDrosophila melanogasterHippo KinasesHippo Signaling PathwayHumansMolecular Sequence DataPhosphorylationProtein BindingAdaptor Proteins, Signal TransducingHippo KinasesLATS1 protein, humanMOB1A protein, humanProtein Serine-Threonine KinasesSerine-Threonine Kinase 3STK3 protein, humanautoinhibitionLats1Mob1Mst2NMRphosphorylationX-ray crystallography

Identifiers

PMID26108669
PMCPMC4511216
OpenAlexW1944684136

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.