ArticleBiology open2015
Novel localization of formin mDia2: importin β-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope.
Article in Biology open, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Nuclear rupture in confined cell migration triggers nuclear actin polymerization to limit chromatin leakage.The EMBO journal · 2025Article
- ERM proteins support perinuclear actin rim formation.Frontiers in cell and developmental biology · 2025Article
- Loss of the importiniScience · 2023Article
- Increased Lamin B1 Levels Promote Cell Migration by Altering Perinuclear Actin Organization.Cells · 2020Article
- The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways.Nature communications · 2020Article
- Geometrical Constraints Greatly Hinder Formin mDia1 Activity.Nano letters · 2020Article
- Imaging within single NPCs reveals NXF1's role in mRNA export on the cytoplasmic side of the pore.The Journal of cell biology · 2019Article
- Actin-Based Cell Protrusion in a 3D Matrix.Trends in cell biology · 2018Review
- Lack of Diaph3 relaxes the spindle checkpoint causing the loss of neural progenitors.Nature communications · 2016Article
- Diaphanous formin mDia2 regulates CENP-A levels at centromeres.The Journal of cell biology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formin family proteins are important regulators of actin polymerization that are involved in many cellular processes. However, little is known about their specific cellular localizations. Here, we show that Diaphanous-related formin-3 (mDia2) localizes to the cytoplasmic side of the nuclear envelope. This localization of mDia2 to the nuclear rim required the presence of a nuclear localization signal (NLS) sequence at the mDia2 N-terminal. Consistent with this result, super-resolution images demonstrated that at the nuclear rim, mDia2 co-localized with the nuclear pore complexes and a nuclear transport receptor, importin β. Furthermore, an interaction between mDia2 and importin β was detected by immunoprecipitation, and silencing of importin β was shown to attenuate accumulation of mDia2 to the nuclear rim. We have shown previously that Ca(2+) entry leads to the assembly of perinuclear actin rim in an inverted formin 2 (INF2) dependent manner. mDia2, however, was not involved in this process since abolishing its localization at the nuclear rim by silencing of importin β had no effect on actin assembly at the nuclear rim triggered by Ca(2+) stimulation.
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