ArticleThe Journal of biological chemistry2009
Differential regulation of actin polymerization and structure by yeast formin isoforms.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Nucleation limits the lengths of actin filaments assembled by formin.Biophysical journal · 2021Article
- Bridging length scales to measure polymer assembly.Molecular biology of the cell · 2017Article
- Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2.Genetics · 2016Article
- The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae.Cellular and molecular life sciences : CMLS · 2016Review
- Importance of a Lys113-Glu195 intermonomer ionic bond in F-actin stabilization and regulation by yeast formins Bni1p and Bnr1p.The Journal of biological chemistry · 2013Article
- Myosin and tropomyosin stabilize the conformation of formin-nucleated actin filaments.The Journal of biological chemistry · 2012Article
- Thoracic aortic aneurysm (TAAD)-causing mutation in actin affects formin regulation of polymerization.The Journal of biological chemistry · 2012Article
- Mutant profilin suppresses mutant actin-dependent mitochondrial phenotype in Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway.Genetics · 2011Review
- Pyrene: a probe to study protein conformation and conformational changes.Molecules (Basel, Switzerland) · 2011Review
- Purification of actin from fission yeast Schizosaccharomyces pombe and characterization of functional differences from muscle actin.The Journal of biological chemistry · 2011Article
- Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance.The Journal of cell biology · 2010Article
- Conformational dynamics of actin: effectors and implications for biological function.Cytoskeleton (Hoboken, N.J.) · 2010Review
- A nucleotide state-sensing region on actin.The Journal of biological chemistry · 2010Article
- Characterization of the biochemical properties and biological function of the formin homology domains of Drosophila DAAM.The Journal of biological chemistry · 2010Article
- Vinculin nucleates actin polymerization and modifies actin filament structure.The Journal of biological chemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The budding yeast formins, Bnr1 and Bni1, behave very differently with respect to their interactions with muscle actin. However, the mechanisms underlying these differences are unclear, and these formins do not interact with muscle actin in vivo. We use yeast wild type and mutant actins to further assess these differences between Bnr1 and Bni1. Low ionic strength G-buffer does not promote actin polymerization. However, Bnr1, but not Bni1, causes the polymerization of pyrene-labeled Mg-G-actin in G-buffer into single filaments based on fluorometric and EM observations. Polymerization by Bnr1 does not occur with Ca-G-actin. By cosedimentation, maximum filament formation occurs at a Bnr1:actin ratio of 1:2. The interaction of Bnr1 with pyrene-labeled S265C Mg-actin yields a pyrene excimer peak, from the cross-strand interaction of pyrene probes, which only occurs in the context of F-actin. In F-buffer, Bnr1 promotes much faster yeast actin polymerization than Bni1. It also bundles the F-actin in contrast to the low ionic strength situation where only single filaments form. Thus, the differences previously observed with muscle actin are not actin isoform-specific. The binding of both formins to F-actin saturate at an equimolar ratio, but only about 30% of each formin cosediments with F-actin. Finally, addition of Bnr1 but not Bni1 to pyrene-labeled wild type and S265C Mg-F actins enhanced the pyrene- and pyrene-excimer fluorescence, respectively, suggesting Bnr1 also alters F-actin structure. These differences may facilitate the ability of Bnr1 to form the actin cables needed for polarized delivery of nutrients and organelles to the growing yeast bud.
Indexed as
Identifiers
What OpenQuestion holds
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.