Evidence map›Paper›PMID 21444821›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins.

Alexander R Paredez, Zoe June Assaf, David Sept, Ljudmilla Timofejeva, Scott C Dawson, Chung-Ju Rachel Wang, W Z Cande

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.9field-weighted citation impact, top 6% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
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  11. Novel Insights into the Wattle and Daub Model ofPathogens (Basel, Switzerland) · 2023
    Article
  12. Review
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  17. Review
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  19. Staging Encystation Progression inFrontiers in cell and developmental biology · 2021
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Alexander R ParedezDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Zoe June Assaf
David Sept
Ljudmilla Timofejeva
Scott C Dawson
Chung-Ju Rachel Wang
W Z Cande
University of California, Berkeley · USTallinn University of Technology · EEUniversity of California, Davis · USUniversity of Michigan–Ann Arbor · US

Funding

PHS HHS A1054693
6 · The paper itself

Abstract

Giardia intestinalis, a human intestinal parasite and member of what is perhaps the earliest-diverging eukaryotic lineage, contains the most divergent eukaryotic actin identified to date and is the first eukaryote known to lack all canonical actin-binding proteins (ABPs). We sought to investigate the properties and functions of the actin cytoskeleton in Giardia to determine whether Giardia actin (giActin) has reduced or conserved roles in core cellular processes. In vitro polymerization of giActin produced filaments, indicating that this divergent actin is a true filament-forming actin. We generated an anti-giActin antibody to localize giActin throughout the cell cycle. GiActin localized to the cortex, nuclei, internal axonemes, and formed C-shaped filaments along the anterior of the cell and a flagella-bundling helix. These structures were regulated with the cell cycle and in encysting cells giActin was recruited to the Golgi-like cyst wall processing vesicles. Knockdown of giActin demonstrated that giActin functions in cell morphogenesis, membrane trafficking, and cytokinesis. Additionally, Giardia contains a single G protein, giRac, which affects the Giardia actin cytoskeleton independently of known target ABPs. These results imply that there exist ancestral and perhaps conserved roles for actin in core cellular processes that are independent of canonical ABPs. Of medical significance, the divergent giActin cytoskeleton is essential and commonly used actin-disrupting drugs do not depolymerize giActin structures. Therefore, the giActin cytoskeleton is a promising drug target for treating giardiasis, as we predict drugs that interfere with the Giardia actin cytoskeleton will not affect the mammalian host.

Indexed as

Evolution, MolecularActinsAnimalsChlorocebus aethiopsCOS CellsCystsCytoskeletonGene Knockdown TechniquesGiardia lambliaGiardiasisHumansIntestinesMicrofilament ProteinsRabbitsActinsMicrofilament Proteins

Identifiers

PMID21444821
PMCPMC3076823
OpenAlexW2002571189

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.