Evidence map›Paper›PMID 20610381›Full record

ArticleThe Journal of biological chemistry2010

Expression of Y53A-actin in Dictyostelium disrupts the cytoskeleton and inhibits intracellular and intercellular chemotactic signaling.

Shi Shu, Xiong Liu, Paul W Kriebel, Myoung-Soon Hong, Mathew P Daniels, Carole A Parent, Edward D Korn

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Actin Tyrosine-53-Phosphorylation in Neuronal Maturation and Synaptic Plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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 3 institutions in 2 countries.

Shi ShuLaboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA.
Xiong Liu
Paul W Kriebel
Myoung-Soon Hong
Mathew P Daniels
Carole A Parent
Edward D Korn
National Institutes of Health · USNational Heart Lung and Blood Institute · USCenter for Cancer Research · US

Funding

Electron Microscopy CoreZICHL005906 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SYED, ZULFEQHAR · 2009 to 2025
$12.9M
Signaling Events Regulating ChemotaxisZIABC010418 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PARENT, CAROLE · 2009 to 2017
$4.6M
Biochemical and Biological Properties of Actins and MyosinsZIAHL000506 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 2009 to 2014
$4.4M
Molecular Basis of Dynamic Localization of Class-I MyosinsZIAHL006035 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 2010 to 2016
$4.4M
Intramural NIH HHS
6 · The paper itself

Abstract

We showed previously that phosphorylation of Tyr(53), or its mutation to Ala, inhibits actin polymerization in vitro with formation of aggregates of short filaments, and that expression of Y53A-actin in Dictyostelium blocks differentiation and development at the mound stage (Liu, X., Shu, S., Hong, M. S., Levine, R. L., and Korn, E. D. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 13694-13699; Liu, X., Shu, S., Hong, M. S., Yu, B., and Korn, E. D. (2010) J. Biol. Chem. 285, 9729-9739). We now show that expression of Y53A-actin, which does not affect cell growth, phagocytosis, or pinocytosis, inhibits the formation of head-to-tail cell streams during cAMP-induced aggregation, although individual amoebae chemotax normally. We show that expression of Y53A-actin causes a 50% reduction of cell surface cAMP receptors, and inhibits cAMP-induced increases in adenylyl cyclase A activity, phosphorylation of ERK2, and actin polymerization. Trafficking of vesicles containing adenylyl cyclase A to the rear of the cell and secretion of the ACA vesicles are also inhibited. The actin cytoskeleton of cells expressing Y53A-actin is characterized by numerous short filaments, and bundled and aggregated filaments similar to the structures formed by copolymerization of purified Y53A-actin and wild-type actin in vitro. This disorganized actin cytoskeleton may be responsible for the inhibition of intracellular and intercellular cAMP signaling in cells expressing F-Y53A-actin.

Indexed as

Gene Expression RegulationActinsAdenylyl CyclasesAmino Acid SequenceCell AdhesionCell LineChemotaxisCytoskeletonDictyosteliumExtracellular SpaceMutationPhosphorylationReceptors, Cyclic AMPSignal TransductionStress, PhysiologicalTransport VesiclesActinsAdenylyl CyclasesReceptors, Cyclic AMPTyrosine

Identifiers

PMID20610381
PMCPMC2934639
OpenAlexW2065261206

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.