Evidence map›Paper›PMID 18689676›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding.

Kyuwon Baek, Xiong Liu, François Ferron, Shi Shu, Edward D Korn, Roberto Dominguez

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  7. Targeting cytoskeletal phosphorylation in cancer.Exploration of targeted anti-tumor therapy · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Actin Tyrosine-53-Phosphorylation in Neuronal Maturation and Synaptic Plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  16. Near-atomic resolution for one state of F-actin.Structure (London, England : 1993) · 2015
    Article
  17. Article
  18. Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. 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

6 authors at 3 institutions in 1 country.

Kyuwon BaekDepartment of Physiology, 3700 Hamilton Walk, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6085, USA.
Xiong Liu
François Ferron
Shi Shu
Edward D Korn
Roberto Dominguez
University of Pennsylvania · USNational Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
REGULATION OF MYOSINS AND MYOSIN KINASES (PAKs)Z01HL000506 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 1985 to 2008
$3.7M
Intramural NIH HHSNCRR NIH HHS P41 RR001646NCRR NIH HHS RR-01646NIGMS NIH HHS DMR-0225180NIGMS NIH HHS GM073791NIGMS NIH HHS R01 GM073791
6 · The paper itself

Abstract

On starvation, Dictyostelium cells aggregate to form multicellular fruiting bodies containing spores that germinate when transferred to nutrient-rich medium. This developmental cycle correlates with the extent of actin phosphorylation at Tyr-53 (pY53-actin), which is low in vegetative cells but high in viable mature spores. Here we describe high-resolution crystal structures of pY53-actin and unphosphorylated actin in complexes with gelsolin segment 1 and profilin. In the structure of pY53-actin, the phosphate group on Tyr-53 makes hydrogen-bonding interactions with residues of the DNase I-binding loop (D-loop) of actin, resulting in a more stable conformation of the D-loop than in the unphosphorylated structures. A more rigidly folded D-loop may explain some of the previously described properties of pY53-actin, including its increased critical concentration for polymerization, reduced rates of nucleation and pointed end elongation, and weak affinity for DNase I. We show here that phosphorylation of Tyr-53 inhibits subtilisin cleavage of the D-loop and reduces the rate of nucleotide exchange on actin. The structure of profilin-Dictyostelium-actin is strikingly similar to previously determined structures of profilin-beta-actin and profilin-alpha-actin. By comparing this representative set of profilin-actin structures with other structures of actin, we highlight the effects of profilin on the actin conformation. In the profilin-actin complexes, subdomains 1 and 3 of actin close around profilin, producing a 4.7 degrees rotation of the two major domains of actin relative to each other. As a result, the nucleotide cleft becomes moderately more open in the profilin-actin complex, probably explaining the stimulation of nucleotide exchange on actin by profilin.

Indexed as

ActinsAnimalsCrystallography, X-RayDictyosteliumHumansModels, MolecularPhosphorylationProfilinsProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryTyrosineActinsProfilinsTyrosine

Identifiers

PMID18689676
PMCPMC2575267
OpenAlexW2167793055

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.