ArticleCommunicative & integrative biology2012
mDia1-3 in mammalian filopodia.
Article in Communicative & integrative biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Constitutively active mDia1 enables visualization of actin assembly in filopodia.bioRxiv : the preprint server for biology · 2026Article
- Chiral growth of adherent filopodia.Biophysical journal · 2023Article
- Plasma membrane phospholipid phosphatase-related proteins as pleiotropic regulators of neuron growth and excitability.Frontiers in molecular neuroscience · 2022Review
- Review
- Emerging regulators of vascular smooth muscle cell migration.Journal of muscle research and cell motility · 2019Review
- Formin and capping protein together embrace the actin filament in a ménage à trois.Nature communications · 2015Article
- Dendritic spine geometry can localize GTPase signaling in neurons.Molecular biology of the cell · 2015Article
- Inhibition of Diaphanous Formin Signaling In Vivo Impairs Cardiovascular Development and Alters Smooth Muscle Cell Phenotype.Arteriosclerosis, thrombosis, and vascular biology · 2015Article
- The diaphanous-related formins promote protrusion formation and cell-to-cell spread of Listeria monocytogenes.The Journal of infectious diseases · 2015Article
- Platelet Rho GTPases-a focus on novel players, roles and relationships.The Biochemical journal · 2015Review
- Short Lives with Long-Lasting Effects: Filopodia Protrusions in Neuronal Branching Morphogenesis.PLoS biology · 2015Article
- Mouse macrophages completely lacking Rho subfamily GTPases (RhoA, RhoB, and RhoC) have severe lamellipodial retraction defects, but robust chemotactic navigation and altered motility.The Journal of biological chemistry · 2014Article
- The actin regulators Enabled and Diaphanous direct distinct protrusive behaviors in different tissues during Drosophila development.Molecular biology of the cell · 2014Article
- Formin' cellular structures: Physiological roles of Diaphanous (Dia) in actin dynamics.Communicative & integrative biology · 2013Review
- The formins FMNL1 and mDia1 regulate coiling phagocytosis of Borrelia burgdorferi by primary human macrophages.Infection and immunity · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
mDia proteins are members of the formin family of actin nucleating proteins that polymerize linear actin filaments. Such filaments form the core of thin, tubular, membrane-bound cell surface protrusions known as filopodia, which are a major feature of mammalian cell morphology. Filopodia are dynamic structures that help cells sense environmental cues, and play a role in cell migration, axon guidance, angiogenesis and other processes. RhoGTPases bind to and control the activity of mDia proteins, and several other binding partners of the three mDia1 isoforms-mDia1, mDia2 and mDia3-have been documented. Two independent pathways controlling mammalian filopodium formation have emerged, with one driven by the RhoGTPase Cdc42, and the other by Rif. While mDia2 has been the main formin implicated in forming filopodia, mDia1 has recently surfaced as the key formin utilized by both the Cdc42 and Rif pathways to drive filopodial protrusion.
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Registered trials
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.