ArticleThe EMBO journal2008
The mammalian formin FHOD1 is activated through phosphorylation by ROCK and mediates thrombin-induced stress fibre formation in endothelial cells.
Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 135 citations in OpenAlex.
- Nuclear Mechanotransduction at the Crossroads: How Membrane Receptors Remodel the Perinuclear Cytoskeleton to Drive Cancer and Disease.International journal of biological sciences · 2026Review
- Tension-sensitive LINC-RhoA signaling prevents chromatin bridge breakage in cytokinesis.The EMBO journal · 2025Article
- The Protein Kinase aPKC as Well as the Small GTPases RhoA and Cdc42 Regulates Neutrophil Chemotaxis Partly by Recruiting the ROCK Kinase to the Leading Edge.Genes to cells : devoted to molecular & cellular mechanisms · 2025Article
- Rho/ROCK Pathway as a Therapeutic Target in Multiple Diseases.International journal of drug discovery and pharmacology · 2025Article
- The expression of the formin Fhod3 in mouse tongue striated muscle.Cell structure and function · 2024Article
- Article
- Macrophage migration is differentially regulated by fibronectin and laminin through altered adhesion and myosin II localization.Molecular biology of the cell · 2024Article
- Characterization of Expression and Function of the Formins FHOD1, INF2, and DAAM1 in HER2-Positive Breast Cancer.Journal of breast cancer · 2023Article
- Direct investigation of cell contraction signal networks by light-based perturbation methods.Pflugers Archiv : European journal of physiology · 2023Review
- FHODs: Nuclear tethered formins for nuclear mechanotransduction.Frontiers in cell and developmental biology · 2023Review
- Actin cytoskeleton in angiogenesis.Biology open · 2022Review
- Angiopoietin-2-induced lymphatic endothelial cell migration drives lymphangiogenesis via the β1 integrin-RhoA-formin axis.Angiogenesis · 2022Article
- Paradigms of endothelial stiffening in cardiovascular disease and vascular aging.Frontiers in physiology · 2022Review
- Neisseria gonorrhoeae subverts formin-dependent actin polymerization to colonize human macrophages.PLoS pathogens · 2021Article
- Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.Structure (London, England : 1993) · 2021Article
- A LINC between the nucleus and the cytoskeleton takes form(in).Structure (London, England : 1993) · 2021Article
- The intercalated disc: a mechanosensing signalling node in cardiomyopathy.Biophysical reviews · 2020Review
- ERK1/2 Phosphorylation of FHOD Connects Signaling and Nuclear Positioning Alternations in Cardiac Laminopathy.Developmental cell · 2019Article
- Article
- Formin proteins in megakaryocytes and platelets: regulation of actin and microtubule dynamics.Platelets · 2019Review
14 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formin-family proteins, in the active state, form actin-based structures such as stress fibres. Their activation mechanisms, however, are largely unknown except that mDia and its closely related formins can be activated by direct binding of the small GTPase Rho or Cdc42. Here we show that the Rho-dependent protein kinase ROCK phosphorylates the C-terminal residues Ser1131, Ser1137, and Thr1141 of formin homology domain protein 1 (FHOD1), a major endothelial formin that is normally autoinhibited by intramolecular interaction between the N- and C-terminal regions. Phosphorylation of FHOD1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. We also demonstrate that, in vascular endothelial cells, thrombin, a vasoactive substance leading to Rho activation, elicits both FHOD1 phosphorylation and stress fibre formation in a ROCK-dependent manner, and that FHOD1 depletion by RNA interference impairs thrombin-induced stress fibre formation. Based on these findings we propose a novel mechanism for activation of formin-family proteins: ROCK, activated by G protein-coupled receptor ligands such as thrombin, directly phosphorylates FHOD1 at the C-terminal region, which renders this formin in the active form, leading to stress fibre formation.
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