Evidence map›Paper›PMID 20631329›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2010

Functional adaptation of the switch-2 nucleotide sensor enables rapid processive translocation by myosin-5.

Nikolett T Nagy, Takeshi Sakamoto, Balázs Takács, Máté Gyimesi, Eszter Hazai, Zsolt Bikádi, James R Sellers, Mihály Kovács

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Switch-2 determines MgFrontiers in physiology · 2024
    Article
  2. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  3. Article
  4. Interplay of actin, ADP and MgArchives of biochemistry and biophysics · 2019
    Article
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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

8 authors at 3 institutions in 2 countries.

Nikolett T NagyDepartment of Biochemistry, Eötvös University, Budapest, Hungary.
Takeshi Sakamoto
Balázs Takács
Máté Gyimesi
Eszter Hazai
Zsolt Bikádi
James R Sellers
Mihály Kovács
Eötvös Loránd University · HUNational Heart Lung and Blood Institute · USVirtua Health · US

Funding

Studies Of Myosin VZIAHL004229 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$2.3M
Emerging New Types of MotilityR01TW007241 · FIC · EOTVOS LORAND UNIVERSITY · PI KOVACS, MIHALY · 2005 to 2009
$260k
FIC NIH HHS 1 R01-TW007241FIC NIH HHS R01 TW007241Howard Hughes Medical Institute
6 · The paper itself

Abstract

Active site loops that are conserved across superfamilies of myosins, kinesins, and G proteins play key roles in allosteric coupling of NTP hydrolysis to interaction with track filaments or effector proteins. In this study, we investigated how the class-specific natural variation in the switch-2 active site loop contributes to the motor function of the intracellular transporter myosin-5. We used single-molecule, rapid kinetic and spectroscopic experiments and semiempirical quantum chemical simulations to show that the class-specific switch-2 structure including a tyrosine (Y439) in myosin-5 enables rapid processive translocation along actin filaments by facilitating Mg(2+)-dependent ADP release. Using wild-type control and Y439 point mutant myosin-5 proteins, we demonstrate that the translocation speed precisely correlates with the kinetics of nucleotide exchange. Switch-2 variants can thus be used to fine-tune translocation speed while maintaining high processivity. The class-specific variation of switch-2 in various NTPase superfamilies indicates its general role in the kinetic tuning of Mg(2+)-dependent nucleotide exchange.

Indexed as

Protein TransportActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsComputer SimulationMagnesiumMiceModels, MolecularMutationMyosin Type VNucleotidesPhosphatesProtein BindingProtein Structure, TertiaryActinsAdenosine DiphosphateAdenosine TriphosphateMagnesiumMyosin Type VNucleotidesPhosphates

Identifiers

PMID20631329
PMCPMC2974419
OpenAlexW1963776092

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.