ArticleMolecular biology of the cell2014
Essential and nonredundant roles for Diaphanous formins in cortical microtubule capture and directed cell migration.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.
What it found
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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.
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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.
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Who cites it
34 citing papers in PubMed, 47 citations in OpenAlex.
- Constitutively active mDia1 enables visualization of actin assembly in filopodia.bioRxiv : the preprint server for biology · 2026Article
- Dissecting cytoskeletal crosstalk through reconstituted actin-microtubule systems.Molecular biology of the cell · 2026Review
- The Rac1-PAK1-Arp2/3 signaling axis regulates CHIKV nsP1-induced filopodia and optimal viral genome replication.Journal of virology · 2024Article
- Article
- mDia formins form hetero-oligomers and cooperatively maintain murine hematopoiesis.PLoS genetics · 2023Article
- Collective dynamics of actin and microtubule and its crosstalk mediated by FHDC1.Frontiers in cell and developmental biology · 2023Article
- Mechanical Forces Govern Interactions of Host Cells with Intracellular Bacterial Pathogens.Microbiology and molecular biology reviews : MMBR · 2022Review
- Review
- iASPP contributes to cell cortex rigidity, mitotic cell rounding, and spindle positioning.The Journal of cell biology · 2021Article
- The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size.Developmental biology · 2021Article
- Diverse Roles of F-BoxProtein3 in Regulation of Various Cellular Functions.Frontiers in cell and developmental biology · 2021Review
- Epithelial morphogenesis, tubulogenesis and forces in organogenesis.Current topics in developmental biology · 2021Review
- Article
- Mammalian diaphanous-related formin 1 (mDia1) coordinates mast cell migration and secretion through its actin-nucleating activity.The Journal of allergy and clinical immunology · 2019Article
- Actin-microtubule crosstalk in cell biology.Nature reviews. Molecular cell biology · 2019Review
- Nuclear Actin Polymerized by mDia2 Confines Centromere Movement during CENP-A Loading.iScience · 2018Article
- Coordination of microtubule acetylation and the actin cytoskeleton by formins.Cellular and molecular life sciences : CMLS · 2018Review
- EB1-binding-myomegalin protein complex promotes centrosomal microtubules functions.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Formin' bridges between microtubules and actin filaments in axonal growth cones.Neural regeneration research · 2017Article
- Adenomatous polyposis coli nucleates actin assembly to drive cell migration and microtubule-induced focal adhesion turnover.The Journal of cell biology · 2017Article
Corrections and comments
- Erratum issuedCorrection.2015
Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
Formins constitute a large family of proteins that regulate the dynamics and organization of both the actin and microtubule cytoskeletons. Previously we showed that the formin mDia1 helps tether microtubules at the cell cortex, acting downstream of the ErbB2 receptor tyrosine kinase. Here we further study the contributions of mDia1 and its two most closely related formins, mDia2 and mDia3, to cortical microtubule capture and ErbB2-dependent breast carcinoma cell migration. We find that depletion of each of these three formins strongly disrupts chemotaxis without significantly affecting actin-based structures. Further, all three formins are required for formation of cortical microtubules in a nonredundant manner, and formin proteins defective in actin polymerization remain active for microtubule capture. Using affinity purification and mass spectrometry analysis, we identify differential binding partners of the formin-homology domain 2 (FH2) of mDia1, mDia2, and mDia3, which may explain their nonredundant roles in microtubule capture. The FH2 domain of mDia1 specifically interacts with Rab6-interacting protein 2 (Rab6IP2). Further, mDia1 is required for cortical localization of Rab6IP2, and concomitant depletion of Rab6IP2 and IQGAP1 severely disrupts cortical capture of microtubules, demonstrating the coinvolvement of mDia1, IQGAP1, and Rab6IP2 in microtubule tethering at the leading edge.
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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.