Evidence map›Paper›PMID 19506755›Full record

ArticlePhysical chemistry chemical physics : PCCP2009

The energetics of allosteric regulation of ADP release from myosin heads.

Del R Jackson, Josh E Baker

Open access · greenAbstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Del R JacksonUniversity of Nevada, Reno, Dept. of Biochemistry, Reno, NV 89557, USA.
Josh E Baker
University of Nevada, Reno · US

Funding

A Multi-Scale Study of the Interplay Between Force Generating and Force Sensing MR01HL090938 · NHLBI · UNIVERSITY OF NEVADA RENO · PI BAKER, JONATHAN E. · 2008 to 2011
$1.3M
Biochemical Screens for Modulators of Muscle ForceR21AR055749 · NIAMS · UNIVERSITY OF NEVADA RENO · PI BAKER, JONATHAN E. · 2008 to 2009
$340k
NHLBI NIH HHS R01HL0909038NHLBI NIH HHS R01 HL090938NIAMS NIH HHS R21 AR055749NIAMS NIH HHS R21AR055749
6 · The paper itself

Abstract

Myosin molecules are involved in a wide range of transport and contractile activities in cells. A single myosin head functions through its ATPase reaction as a force generator and as a mechanosensor, and when two or more myosin heads work together in moving along an actin filament, the interplay between these mechanisms contributes to collective myosin behaviors. For example, the interplay between force-generating and force-sensing mechanisms coordinates the two heads of a myosin V molecule in its hand-over-hand processive stepping along an actin filament. In muscle, it contributes to the Fenn effect and smooth muscle latch. In both examples, a key force-sensing mechanism is the regulation of ADP release via interhead forces that are generated upon actin-myosin binding. Here we present a model describing the mechanism of allosteric regulation of ADP release from myosin heads as a change, DeltaDeltaG(-D), in the standard free energy for ADP release that results from the work, Deltamicro(mech), performed by that myosin head upon ADP release, or DeltaDeltaG(-D) = Deltamicro(mech). We show that this model is consistent with previous measurements for strain-dependent kinetics of ADP release in both myosin V and muscle myosin II. The model makes explicit the energetic cost of accelerating ADP release, showing that acceleration of ADP release during myosin V processivity requires approximately 4 kT of energy whereas the energetic cost for accelerating ADP release in a myosin II-based actin motility assay is only approximately 0.4 kT. The model also predicts that the acceleration of ADP release involves a dissipation of interhead forces. To test this prediction, we use an in vitro motility assay to show that the acceleration of ADP release from both smooth and skeletal muscle myosin II correlates with a decrease in interhead force. Our analyses provide clear energetic constraints for models of the allosteric regulation of ADP release and provide novel, testable insights into muscle and myosin V function.

Indexed as

ActinsAdenosine DiphosphateAllosteric RegulationAnimalsChickensKineticsModels, MolecularMyosinsRotationThermodynamicsActinsAdenosine DiphosphateMyosins

Identifiers

PMID19506755
PMCPMC2767480
OpenAlexW2071799308

What OpenQuestion holds

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LicenceTDM
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.