ArticleThe Journal of biological chemistry2008
Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- The amount of Nck rather than N-WASP correlates with the rate of actin-based motility of Vaccinia virus.Microbiology spectrum · 2023Article
- Unconcerted conformational changes in Arp2/3 complex integrate multiple activating signals to assemble functional actin networks.Current biology : CB · 2022Article
- Reversible Kinetic Trapping of FUS Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Entropy-driven translocation of disordered proteins through the Gram-positive bacterial cell wall.Nature microbiology · 2021Article
- Review
- WH2 and proline-rich domains of WASP-family proteins collaborate to accelerate actin filament elongation.The EMBO journal · 2018Article
- Genetic subtyping of Listeria monocytogenes via multiple-locus sequence typing using iap, sigB and actA.The Journal of veterinary medical science · 2017Article
- Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein.The Journal of biological chemistry · 2015Article
- Biophysical properties of intrinsically disordered p130Cas substrate domain--implication in mechanosensing.PLoS computational biology · 2014Article
- Three-dimensional architecture of actin filaments in Listeria monocytogenes comet tails.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Control of actin-based motility through localized actin binding.Physical biology · 2013Article
- Article
- Article
- Actin filament attachments for sustained motility in vitro are maintained by filament bundling.PloS one · 2012Article
- Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Mechanism of a concentration-dependent switch between activation and inhibition of Arp2/3 complex by coronin.The Journal of biological chemistry · 2011Article
- Molecular mechanism of Ena/VASP-mediated actin-filament elongation.The EMBO journal · 2011Article
- Physical mechanisms of signal integration by WASP family proteins.Annual review of biochemistry · 2010Review
- Listeria monocytogenes ActA-mediated escape from autophagic recognition.Nature cell biology · 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
3 authors at 2 institutions in 1 country.
Funding
Abstract
Studies of the biochemistry of Listeria monocytogenes virulence protein ActA have typically focused on the behavior of bacteria in complex systems or on the characterization of the protein after expression and purification. Although prior in vivo work has proposed that ActA forms dimers on the surface of L. monocytogenes, dimerization has not been demonstrated in vitro, and little consideration has been given to the surface environment where ActA performs its pivotal role in bacterial actin-based motility. We have synthesized and characterized an ActA dimer and provide evidence that the two ActA molecules do not interact with each other even when tethered together. However, we also demonstrate that artificial dimers provide superior activation of actin nucleation by the Arp2/3 complex compared with monomers and that increased activation of the Arp2/3 complex by dimers may be a general property of Arp2/3 activators. It appears that the close packing ( approximately 19 nm) of ActA molecules on the surface of L. monocytogenes is so dense that the kinetics of actin nucleation mimic that of synthetic ActA dimers. We also present observations indicating that ActA is a natively unfolded protein, largely random coil that is responsible for many of the unique physical properties of ActA including its extended structure, aberrant mobility during SDS-PAGE, and ability to resist irreversible denaturation upon heating.
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.