Evidence map›Paper›PMID 20530485›Full record

ArticleThe Journal of biological chemistry2010

A nucleotide state-sensing region on actin.

Dmitri S Kudryashov, Elena E Grintsevich, Peter A Rubenstein, Emil Reisler

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2022
    Article
  4. Article
  5. International journal of molecular sciences · 2021
    Article
  6. Article
  7. Article
  8. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Article
  11. ATP and ADP actin states.Biopolymers · 2013
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Dmitri S KudryashovDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA. dkudryas@ucla.edu
Elena E Grintsevich
Peter A Rubenstein
Emil Reisler
University of California, Los Angeles · USUniversity of Iowa · US

Funding

Dynamic Events in Myosin and Actin and Their FunctionR01GM077190 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 2006 to 2020
$6.2M
MUTAGENIC STUDY OF YEAST ACTIN CONFORMATIONAL CHANGESR01GM033689 · NIGMS · UNIVERSITY OF IOWA · PI RUBENSTEIN, PETER A. · 1985 to 2010
$3.7M
NIGMS NIH HHS GM077190NIGMS NIH HHS GM33689NIGMS NIH HHS R01 GM033689NIGMS NIH HHS R01 GM077190
6 · The paper itself

Abstract

The nucleotide state of actin (ATP, ADP-P(i), or ADP) is known to impact its interactions with other actin molecules upon polymerization as well as with multiple actin binding proteins both in the monomeric and filamentous states of actin. Recently, molecular dynamics simulations predicted that a sequence located at the interface of subdomains 1 and 3 (W-loop; residues 165-172) changes from an unstructured loop to a beta-turn conformation upon ATP hydrolysis (Zheng, X., Diraviyam, K., and Sept, D. (2007) Biophys. J. 93, 1277-1283). This region participates directly in the binding to other subunits in F-actin as well as to cofilin, profilin, and WH2 domain proteins and, therefore, could contribute to the nucleotide sensitivity of these interactions. The present study demonstrates a reciprocal communication between the W-loop region and the nucleotide binding cleft on actin. Point mutagenesis of residues 167, 169, and 170 and their site-specific labeling significantly affect the nucleotide release from the cleft region, whereas the ATP/ADP switch alters the fluorescence of probes located in the W-loop. In the ADP-P(i) state, the W-loop adopts a conformation similar to that in the ATP state but different from the ADP state. Binding of latrunculin A to the nucleotide cleft favors the ATP-like conformation of the W-loop, whereas ADP-ribosylation of Arg-177 forces the W-loop into a conformation distinct from those in the ADP and ATP-states. Overall, our experimental data suggest that the W-loop of actin is a nucleotide sensor, which may contribute to the nucleotide state-dependent changes in F-actin and nucleotide state-modulated interactions of both G- and F-actin with actin-binding proteins.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateBridged Bicyclo Compounds, HeterocyclicMicroscopy, ElectronMutagenesis, Site-DirectedMutationNucleotidesProtein Structure, SecondaryThiazolidinesYeastsActinsAdenosine DiphosphateAdenosine TriphosphateBridged Bicyclo Compounds, Heterocycliclatrunculin ANucleotidesThiazolidines

Identifiers

PMID20530485
PMCPMC2919123
OpenAlexW2059308008

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.