Evidence map›Paper›PMID 22713570›Full record

ArticleBiophysical journal2012

Switch II mutants reveal coupling between the nucleotide- and actin-binding regions in myosin V.

Darshan V Trivedi, Charles David, Donald J Jacobs, Christopher M Yengo

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Interplay of actin, ADP and MgArchives of biochemistry and biophysics · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

4 authors at 2 institutions in 1 country.

Darshan V TrivediDepartment of Cellular and Molecular Physiology, College of Medicine, Pennsylvania State University, Hershey, Pennsylvania, USA.
Charles David
Donald J Jacobs
Christopher M Yengo
Pennsylvania State University · USUniversity of North Carolina at Charlotte · US

Funding

Predicting protein flexibility and stabilityR01GM073082 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI JACOBS, DONALD · 2006 to 2010
$1.6M
Enzymatic and Motor Properties of Myosin IIIR01EY018141 · NEI · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI YENGO, CHRISTOPHER M · 2008 to 2012
$1.3M
Energy Transduction in MyosinR21HL093531 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI YENGO, CHRISTOPHER M · 2009 to 2010
$390k
NEI NIH HHS EY018141NEI NIH HHS R01 EY018141NHLBI NIH HHS HL093531NHLBI NIH HHS R21 HL093531NIGMS NIH HHS GM073082NIGMS NIH HHS R01 GM073082
6 · The paper itself

Abstract

Conserved active-site elements in myosins and other P-loop NTPases play critical roles in nucleotide binding and hydrolysis; however, the mechanisms of allosteric communication among these mechanoenzymes remain unresolved. In this work we introduced the E442A mutation, which abrogates a salt-bridge between switch I and switch II, and the G440A mutation, which abolishes a main-chain hydrogen bond associated with the interaction of switch II with the γ phosphate of ATP, into myosin V. We used fluorescence resonance energy transfer between mant-labeled nucleotides or IAEDANS-labeled actin and FlAsH-labeled myosin V to examine the conformation of the nucleotide- and actin-binding regions, respectively. We demonstrate that in the absence of actin, both the G440A and E442A mutants bind ATP with similar affinity and result in only minor alterations in the conformation of the nucleotide-binding pocket (NBP). In the presence of ADP and actin, both switch II mutants disrupt the formation of a closed NBP actomyosin.ADP state. The G440A mutant also prevents ATP-induced opening of the actin-binding cleft. Our results indicate that the switch II region is critical for stabilizing the closed NBP conformation in the presence of actin, and is essential for communication between the active site and actin-binding region.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsBinding SitesChickensCrystallography, X-RayFluorescence Resonance Energy TransferKineticsModels, MolecularMutant ProteinsMyosin Type VNucleotidesProtein BindingProtein Structure, SecondaryTemperatureActinsAdenosine DiphosphateAdenosine TriphosphateMutant ProteinsMyosin Type VNucleotides

Identifiers

PMID22713570
PMCPMC3368122
OpenAlexW1986969900

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.