p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
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Rho small GTPase regulates cell morphology, adhesion and cytokinesis through the actin cytoskeleton. We have identified a protein, p140mDia, as a downstream effector of Rho. It is a mammalian homolog of Drosophila diaphanous, a protein required for cytokinesis, and belongs to a family of formin-related proteins containing repetitive polyproline stretches. p140mDia binds selectively to the GTP-bound form of Rho and also binds to profilin. p140mDia, profilin and RhoA are co-localized in the spreading lamellae of cultured fibroblasts. They are also co-localized in membrane ruffles of phorbol ester-stimulated sMDCK2 cells, which extend these structures in a Rho-dependent manner. The three proteins are recruited around phagocytic cups induced by fibronectin-coated beads. Their recruitment is not induced after Rho is inactivated by microinjection of botulinum C3 exoenzyme. Overexpression of p140mDia in COS-7 cells induced homogeneous actin filament formation. These results suggest that Rho regulates actin polymerization by targeting profilin via p140mDia beneath the specific plasma membranes.
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mDia is a formin molecule that catalyzes actin nucleation and polymerization through its interaction with profilin.
“mDia is a formin molecule that catalyzes actin nucleation and polymerization through its interaction with the actin-binding protein profilin [121].”
From RhoA Signaling in Neurodegenerative Diseases (2022) · cites this paper as [121]
In the section on activation-dependent clustering (page unavailable), the paper identifies p140mDia as a formin-related protein and proposes that it recruits profilin to sites where actin polymerization occurs. It reports enhanced actin filament assembly with p140mDia overexpression, but says whether p140mDia influences profilin-catalyzed polymerization remains to be investigated. It does not establish that mDia catalyzes actin nucleation or polymerization through profilin. (LLM, conf=0.90)
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- Authors
- Watanabe, N., Madaule, P., Reid, T., Ishizaki, T., Watanabe, G., Kakizuka, A., Saito, Y., Nakao, K., Jockusch, B. M., & Narumiya, S.
- Affiliations
- Kyoto University (JP)
- Technische Universität Braunschweig (DE)
- Corresponding author
- Narumiya, Shuh
- ORCID
- Nakao, Kazuwa
- Venue
- The EMBO Journal
- Published
- 1997-06-01
- Volume
- 16
- Issue
- 11
- Pages
- 3044-3056
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1169923
- OpenAlex
- W2139582633
- Cited by
- 823
- References
- 1
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 10 · 2023: 9 · 2022: 15 · 2021: 19 · 2020: 19 · 2019: 27 · 2018: 15 · 2017: 16 · 2016: 11 · 2015: 23 · 2014: 22 · 2013: 28 · 2012: 34
- FWCI
- 17.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Diaphanous, RhoA, profilin, Rho GTPases, actin polymerization, actin cytoskeleton, cytokinesis, phagocytosis, ruffles, lamellae, fibroblasts
- MeSH terms
- Formins, Amino Acid Sequence, Animals, Carrier Proteins, Cell Adhesion, Cell Membrane, Cell Movement, Contractile Proteins, Drosophila, Fluorescent Antibody Technique, Fungal Proteins, Ligands, Microfilament Proteins, Molecular Sequence Data, Protein Binding, Recombinant Proteins, 3T3 Cells, Sequence Homology, Amino Acid, GTP-Binding Proteins, Insect Proteins, rhoA GTP-Binding Protein, Saccharomyces cerevisiae Proteins, Drosophila Proteins, Profilins, Mice
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