Evidence map›Paper›PMID 27758857›Full record

ArticleThe Journal of biological chemistry2016

Structure of the Shroom-Rho Kinase Complex Reveals a Binding Interface with Monomeric Shroom That Regulates Cell Morphology and Stimulates Kinase Activity.

Jenna K Zalewski, Joshua H Mo, Simone Heber, Annie Heroux, Richard G Gardner, Jeffrey D Hildebrand, Andrew P VanDemark

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% of its field
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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026
    Review
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  9. Suppression ofInternational journal of molecular sciences · 2020
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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

7 authors at 3 institutions in 1 country.

Jenna K ZalewskiFrom the Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260.
Joshua H MoFrom the Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260.
Simone HeberFrom the Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260.
Annie Herouxthe Department of Biology, Brookhaven National Laboratory, Upton, New York 11973, and.
Richard G Gardnerthe Department of Pharmacology, University of Washington, Seattle, Washington 98195.
Jeffrey D HildebrandFrom the Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260.
Andrew P VanDemarkFrom the Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, andyv@pitt.edu.
University of Pittsburgh · USBrookhaven National Laboratory · USUniversity of Washington · US

Funding

The Structural Basis of Shroom-Mediated Cell ContractilityR01GM097204 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI VANDEMARK, ANDREW PAUL · 2011 to 2015
$1.4M
NIGMS NIH HHS R01 GM097204
6 · The paper itself

Abstract

Shroom-mediated remodeling of the actomyosin cytoskeleton is a critical driver of cellular shape and tissue morphology that underlies the development of many tissues including the neural tube, eye, intestines, and vasculature. Shroom uses a conserved SD2 domain to direct the subcellular localization of Rho-associated kinase (Rock), which in turn drives changes in the cytoskeleton and cellular morphology through its ability to phosphorylate and activate non-muscle myosin II. Here, we present the structure of the human Shroom-Rock binding module, revealing an unexpected stoichiometry for Shroom in which two Shroom SD2 domains bind independent surfaces on Rock. Mutation of interfacial residues impaired Shroom-Rock binding in vitro and resulted in altered remodeling of the cytoskeleton and loss of Shroom-mediated changes in cellular morphology. Additionally, we provide the first direct evidence that Shroom can function as a Rock activator. These data provide molecular insight into the Shroom-Rock interface and demonstrate that Shroom directly participates in regulating cytoskeletal dynamics, adding to its known role in Rock localization.

Indexed as

G-Protein-Coupled Receptor Kinase 1HumansMembrane ProteinsMicrofilament ProteinsMultiprotein ComplexesMyosin Type IIProtein DomainsProtein Structure, QuaternaryStructure-Activity RelationshipG-Protein-Coupled Receptor Kinase 1GRK1 protein, humanMembrane ProteinsMicrofilament ProteinsMultiprotein ComplexesMyosin Type IIShroom1 protein, humancoiled-coilcytoskeletonRas homolog gene family, member A (RhoA)RhoARho-kinaseserine/threonine protein kinaseShroomstructural biologyX-ray crystallography

Identifiers

PMID27758857
PMCPMC5207239
OpenAlexW2530496880

What OpenQuestion holds

Textmetadata
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.