ArticleTraffic (Copenhagen, Denmark)2008
Arp11 affects dynein-dynactin interaction and is essential for dynein function in Aspergillus nidulans.
Article in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 35 citations in OpenAlex.
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.Cell reports · 2024Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024Article
- Microtubule association of TRIM3 revealed by differential extraction proteomics.Journal of cell science · 2024Article
- Dynein activation in vivo is regulated by the nucleotide states of its AAA3 domain.Current biology : CB · 2021Article
- Article
- The splicing-factor Prp40 affects dynein-dynactin function inMolecular biology of the cell · 2020Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
- LIS1 regulates cargo-adapter-mediated activation of dynein by overcoming its autoinhibition in vivo.The Journal of cell biology · 2019Article
- p25 of the dynactin complex plays a dual role in cargo binding and dynactin regulation.The Journal of biological chemistry · 2018Article
- Nuclear movement in fungi.Seminars in cell & developmental biology · 2018Review
- The actin capping protein in Aspergillus nidulans enhances dynein function without significantly affecting Arp1 filament assembly.Scientific reports · 2018Article
- Dynein/dynactin is necessary for anterograde transport ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Regulation of mitochondria-dynactin interaction and mitochondrial retrograde transport in axons.eLife · 2017Article
- Discovery of a vezatin-like protein for dynein-mediated early endosome transport.Molecular biology of the cell · 2015Article
- Cytoplasmic dynein and early endosome transport.Cellular and molecular life sciences : CMLS · 2015Review
- In vitro screen of prion disease susceptibility genes using the scrapie cell assay.Human molecular genetics · 2014Article
- HookA is a novel dynein-early endosome linker critical for cargo movement in vivo.The Journal of cell biology · 2014Article
- Identification of a novel site in the tail of dynein heavy chain important for dynein function in vivo.The Journal of biological chemistry · 2013Article
- Dynactin's pointed-end complex is a cargo-targeting module.Molecular biology of the cell · 2012Article
- In vivo roles of the basic domain of dynactin p150 in microtubule plus-end tracking and dynein function.Traffic (Copenhagen, Denmark) · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The dynactin complex contains proteins including p150 that interacts with cytoplasmic dynein and an actin-related protein Arp1 that forms a minifilament. Proteins including Arp11 and p62 locate at the pointed end of the Arp1 filament, but their biochemical functions are unclear (Schroer TA. Dynactin. Annu Rev Cell Dev Biol 2004;20:759-779). In Aspergillus nidulans, loss of Arp11 or p62 causes the same nuclear distribution (nud) defect displayed by dynein mutants, indicating that these pointed-end proteins are essential for dynein function. We constructed a strain with S-tagged p150 of dynactin that allows us to pull down components of the dynactin and dynein complexes. Surprisingly, while the ratio of pulled-down Arp1 to S-p150 in Arp11-depleted cells is clearly lower than that in wild-type cells, the ratio of pulled-down dynein to S-p150 is significantly higher. We further show that the enhanced dynein-dynactin interaction in Arp11-depleted cells is also present in the soluble fraction and therefore is not dependent upon the affinity of these proteins to the membrane. We suggest that loss of the pointed-end proteins alters the Arp1 filament in a way that affects the conformation of p150 required for its proper interaction with the dynein motor.
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.