ArticleJournal of cell science2009
INF2 is an endoplasmic reticulum-associated formin protein.
Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 139 citations in OpenAlex.
- Phosphorylation-dependent interaction between VAP proteins and INF2 influences ER morphology.Current biology : CB · 2026Article
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- Patient-specific hiPSC-Podocytes as an in vitro model of genetic FSGS.Scientific reports · 2025Article
- Spatial proteomics of ER tubules reveals CLMN, an ER-actin tether at focal adhesions that promotes cell migration.Cell reports · 2025Article
- The activation of INF2 by Piezo1/CaCurrent biology : CB · 2025Article
- SUN2 mediates calcium-triggered nuclear actin polymerization to cluster active RNA polymerase II.EMBO reports · 2024Article
- Altered Endoplasmic Reticulum Integrity and Organelle Interactions in Living Cells Expressing INF2 Variants.International journal of molecular sciences · 2024Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.The Journal of cell biology · 2024Article
- INF2 formin variants linked to human inherited kidney disease reprogram the transcriptome, causing mitotic chaos and cell death.Cellular and molecular life sciences : CMLS · 2024Article
- FMNL2 regulates actin for endoplasmic reticulum and mitochondria distribution in oocyte meiosis.eLife · 2024Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.bioRxiv : the preprint server for biology · 2024Article
- The activation of INF2 by Piezo1/CabioRxiv : the preprint server for biology · 2024Article
- Cell type-specific regulation of CFTR trafficking-on the verge of progress.Frontiers in cell and developmental biology · 2024Review
- Convergent and divergent mechanisms of peroxisomal and mitochondrial division.The Journal of cell biology · 2023Article
- Characterization of cytoskeletal and structural effects of INF2 variants causing glomerulopathy and neuropathy.Scientific reports · 2023Article
- Structure and function of the N-terminal extension of the formin INF2.Cellular and molecular life sciences : CMLS · 2022Article
- INF2-mediated actin filament reorganization confers intrinsic resilience to neuronal ischemic injury.Nature communications · 2022Article
- Review
- Myosin II proteins are required for organization of calcium-induced actin networks upstream of mitochondrial division.Molecular biology of the cell · 2022Article
- Shielding of actin by the endoplasmic reticulum impacts nuclear positioning.Nature communications · 2022Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In addition to its ability to accelerate filament assembly, which is common to formins, INF2 is a formin protein with the unique biochemical ability to accelerate actin filament depolymerization. The depolymerization activity of INF2 requires its actin monomer-binding WASP homology 2 (WH2) motif. In this study, we show that INF2 is peripherally bound to the cytoplasmic face of the endoplasmic reticulum (ER) in Swiss 3T3 cells. Both endogenous INF2 and GFP-fusion constructs display ER localization. INF2 is post-translationally modified by a C-terminal farnesyl group, and this modification is required for ER interaction. However, farnesylation is not sufficient for ER association, and membrane extraction experiments suggest that ionic interactions are also important. The WH2 motif also serves as a diaphanous autoregulatory domain (DAD), which binds to the N-terminal diaphanous inhibitory domain (DID), with an apparent dissociation constant of 1.1 muM. Surprisingly, the DID-DAD interaction does not inhibit the actin nucleation activity of INF2; however, it does inhibit the depolymerization activity. Point mutations to the DAD/WH2 inhibit both the DID-DAD interaction and depolymerization activity. Expression of GFP-INF2 containing these DAD/WH2 mutations causes the ER to collapse around the nucleus, with accumulation of actin filaments around the collapsed ER. This study is the first to show the association of an actin-assembly factor with the ER.
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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.