Evidence map›Paper›PMID 24637024›Full record

ArticleThe Journal of biological chemistry2014

Molecular characterization and subcellular localization of Arabidopsis class VIII myosin, ATM1.

Takeshi Haraguchi, Motoki Tominaga, Rie Matsumoto, Kei Sato, Akihiko Nakano, Keiichi Yamamoto, Kohji Ito

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

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  15. Discovery of ultrafast myosin, its amino acid sequence, and structural features.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

7 authors at 3 institutions in 1 country.

Takeshi HaraguchiFrom the Department of Biology, Graduate School of Science, Chiba University, Inage-ku, Chiba 263-8522.
Motoki Tominaga
Rie Matsumoto
Kei Sato
Akihiko Nakano
Keiichi Yamamoto
Kohji Ito
Chiba University · JPThe University of Tokyo · JPRIKEN Center for Advanced Photonics · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Land plants possess myosin classes VIII and XI. Although some information is available on the molecular properties of class XI myosins, class VIII myosins are not characterized. Here, we report the first analysis of the enzymatic properties of class VIII myosin. The motor domain of Arabidopsis class VIII myosin, ATM1 (ATM1-MD), and the motor domain plus one IQ motif (ATM1-1IQ) were expressed in a baculovirus system and characterized. ATM1-MD and ATM1-1IQ had low actin-activated Mg(2+)-ATPase activity (Vmax = 4 s(-1)), although their affinities for actin were high (Kactin = 4 μM). The actin-sliding velocities of ATM1-MD and ATM1-1IQ were 0.02 and 0.089 μm/s, respectively, from which the value for full-length ATM1 is calculated to be ∼0.2 μm/s. The results of actin co-sedimentation assay showed that the duty ratio of ATM1 was ∼90%. ADP dissociation from the actin·ATM1 complex (acto-ATM1) was extremely slow, which accounts for the low actin-sliding velocity, low actin-activated ATPase activity, and high duty ratio. The rate of ADP dissociation from acto-ATM1 was markedly biphasic with fast and slow phase rates (5.1 and 0.41 s(-1), respectively). Physiological concentrations of free Mg(2+) modulated actin-sliding velocity and actin-activated ATPase activity by changing the rate of ADP dissociation from acto-ATM1. GFP-fused full-length ATM1 expressed in Arabidopsis was localized to plasmodesmata, plastids, newly formed cell walls, and actin filaments at the cell cortex. Our results suggest that ATM1 functions as a tension sensor/generator at the cell cortex and other structures in Arabidopsis.

Indexed as

Actin CytoskeletonActinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateArabidopsisArabidopsis ProteinsDinitrobenzenesGreen Fluorescent ProteinsKineticsMicroscopy, ConfocalMyosinsPlants, Genetically ModifiedProtein BindingProtoplastsSulfanilamidesActinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateArabidopsis ProteinsATM1 class VIII myosin, ArabidopsisDinitrobenzenesGreen Fluorescent ProteinsMyosinsoryzalinSulfanilamidesTubulin ModulatorsActinArabidopsisATPasesKineticsMolecular MotorsMyosin

Identifiers

PMID24637024
PMCPMC4007431
OpenAlexW2090922453

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.