ArticleMolecular biology of the cell2012
Structure of Shroom domain 2 reveals a three-segmented coiled-coil required for dimerization, Rock binding, and apical constriction.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Decoding the Evolution and Co-Phospho-Regulatory Networks of SHROOM Proteins.Journal of molecular evolution · 2026Article
- Mapping Shroom3 expression across the adult mouse.Gene expression patterns : GEP · 2025Article
- Alternative Splicing in Mechanically Stretched Podocytes as a Model of Glomerular Hypertension.Journal of the American Society of Nephrology : JASN · 2025Article
- The Critical Role of the Shroom Family Proteins in Morphogenesis, Organogenesis and Disease.Phenomics (Cham, Switzerland) · 2024Review
- The Good and the Bad of SHROOM3 in Kidney Development and Disease: A Narrative Review.Canadian journal of kidney health and disease · 2023Review
- Rosette morphology in zona glomerulosa formation and function.Molecular and cellular endocrinology · 2021Review
- A modifier screen identifies regulators of cytoskeletal architecture as mediators of Shroom-dependent changes in tissue morphology.Biology open · 2021Article
- β-Catenin and FGFR2 regulate postnatal rosette-based adrenocortical morphogenesis.Nature communications · 2020Article
- SHROOM2 inhibits tumor metastasis through RhoA-ROCK pathway-dependent and -independent mechanisms in nasopharyngeal carcinoma.Cell death & disease · 2019Article
- Scoria: a Python module for manipulating 3D molecular data.Journal of cheminformatics · 2017Article
- Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins.Journal of visualized experiments : JoVE · 2017Article
- Accurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning Model.PLoS computational biology · 2017Article
- Structure of the Shroom-Rho Kinase Complex Reveals a Binding Interface with Monomeric Shroom That Regulates Cell Morphology and Stimulates Kinase Activity.The Journal of biological chemistry · 2016Article
- Apical Sarcomere-like Actomyosin Contracts Nonmuscle Drosophila Epithelial Cells.Developmental cell · 2016Article
- Coiled-coils: The long and short of it.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016Review
- Made to measure - keeping Rho kinase at a distance.Small GTPases · 2016Review
- A molecular ruler regulates cytoskeletal remodelling by the Rho kinases.Nature communications · 2015Article
- Targeted inhibition of the Shroom3-Rho kinase protein-protein interaction circumvents Nogo66 to promote axon outgrowth.BMC neuroscience · 2015Article
- Shroom3 functions downstream of planar cell polarity to regulate myosin II distribution and cellular organization during neural tube closure.Biology open · 2015Article
- The interaction between Shroom3 and Rho-kinase is required for neural tube morphogenesis in mice.Biology open · 2014Article
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Authors and funding
8 authors.
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Abstract
Shroom (Shrm) proteins are essential regulators of cell shape and tissue morpho-logy during animal development that function by interacting directly with the coiled-coil region of Rho kinase (Rock). The Shrm-Rock interaction is sufficient to direct Rock subcellular localization and the subsequent assembly of contractile actomyosin networks in defined subcellular locales. However, it is unclear how the Shrm-Rock interaction is regulated at the molecular level. To begin investigating this issue, we present the structure of Shrm domain 2 (SD2), which mediates the interaction with Rock and is required for Shrm function. SD2 is a unique three-segmented dimer with internal symmetry, and we identify conserved residues on the surface and within the dimerization interface that are required for the Rock-Shrm interaction and Shrm activity in vivo. We further show that these residues are critical in both vertebrate and invertebrate Shroom proteins, indicating that the Shrm-Rock signaling module has been functionally and molecularly conserved. The structure and biochemical analysis of Shrm SD2 indicate that it is distinct from other Rock activators such as RhoA and establishes a new paradigm for the Rock-mediated assembly of contractile actomyosin networks.
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