ArticleThe Journal of biological chemistry2015
Assembly and turnover of short actin filaments by the formin INF2 and profilin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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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Who cites it
27 citing papers in PubMed, 36 citations in OpenAlex.
- AAV2 Crosslinks Actin Filaments: Implications for AAV Gene Therapy Vector Design.bioRxiv : the preprint server for biology · 2026Article
- Mitochondrial Calcium Signaling in Hepatocyte Health and Disease.Cold Spring Harbor perspectives in biology · 2026Review
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- Formin 3 stabilizes the cytoskeleton of Drosophila tendon cells, thus enabling them to resist muscle tensile forces.Journal of cell science · 2025Article
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Article
- The actin binding protein profilin 1 localizes inside mitochondria and is critical for their function.EMBO reports · 2024Article
- The actin binding protein profilin 1 is critical for mitochondria function.bioRxiv : the preprint server for biology · 2023Article
- Parallel actin monomers in the 8S complex of actin-INF2.Journal of biomolecular structure & dynamics · 2023Article
- Biomechanical, biophysical and biochemical modulators of cytoskeletal remodelling and emergent stem cell lineage commitment.Communications biology · 2023Review
- Unveiling the potential of mitochondrial dynamics as a therapeutic strategy for acute kidney injury.Frontiers in cell and developmental biology · 2023Review
- Bring the pain: wounding reveals a transition from cortical excitability to epithelial excitability inFrontiers in cell and developmental biology · 2023Review
- Mff oligomerization is required for Drp1 activation and synergy with actin filaments during mitochondrial division.Molecular biology of the cell · 2021Article
- Kinesin-6 Klp9 orchestrates spindle elongation by regulating microtubule sliding and growth.eLife · 2021Article
- Profilin 1 and Mitochondria-Partners in the Pathogenesis of Coronary Artery Disease?International journal of molecular sciences · 2021Review
- Players in Mitochondrial Dynamics and Female Reproduction.Frontiers in molecular biosciences · 2021Review
- FSGS-Causing INF2 Mutation Impairs Cleaved INF2 N-Fragment Functions in Podocytes.Journal of the American Society of Nephrology : JASN · 2020Article
- Regulation of INF2-mediated actin polymerization through site-specific lysine acetylation of actin itself.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly.iScience · 2019Article
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
INF2 (inverted formin 2) is a formin protein with unique biochemical effects on actin. In addition to the common formin ability to accelerate actin nucleation and elongation, INF2 can also sever filaments and accelerate their depolymerization. Although we understand key attributes of INF2-mediated severing, we do not understand the mechanism by which INF2 accelerates depolymerization subsequent to severing. Here, we show that INF2 can create short filaments (<60 nm) that continuously turn over actin subunits through a combination of barbed end elongation, severing, and WH2 motif-mediated depolymerization. This pseudo-steady state condition occurs whether starting from actin filaments or monomers. The rate-limiting step of the cycle is nucleotide exchange of ADP for ATP on actin monomers after release from the INF2/actin complex. Profilin addition has two effects: 1) to accelerate filament turnover 6-fold by accelerating nucleotide exchange and 2) to shift the equilibrium toward polymerization, resulting in longer filaments. In sum, our findings show that the combination of multiple interactions of INF2 with actin can work in concert to increase the ATP turnover rate of actin. Depending on the ratio of INF2:actin, this increased flux can result in rapid filament depolymerization or maintenance of short filaments. We also show that high concentrations of cytochalasin D accelerate ATP turnover by actin but through a different mechanism from that of INF2.
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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.