Evidence map›Paper›PMID 23990465›Full record

ArticleThe Journal of biological chemistry2013

Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3.

Manuel H Taft, Elmar Behrmann, Lena-Christin Munske-Weidemann, Claudia Thiel, Stefan Raunser, Dietmar J Manstein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

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  11. Myosin 18Aα targets the guanine nucleotide exchange factor β-Pix to the dendritic spines of cerebellar Purkinje neurons and promotes spine maturation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
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  12. Review
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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

6 authors at 2 institutions in 1 country.

Manuel H TaftFrom the Institute for Biophysical Chemistry, Hannover Medical School, OE 4350, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany and. Electronic address: Taft.Manuel@MH-Hannover.de.
Elmar Behrmannthe Department of Physical Biochemistry, Max-Planck-Institute of Molecular Physiology, 44227 Dortmund, Germany.
Lena-Christin Munske-WeidemannFrom the Institute for Biophysical Chemistry, Hannover Medical School, OE 4350, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany and.
Claudia ThielFrom the Institute for Biophysical Chemistry, Hannover Medical School, OE 4350, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany and.
Stefan Raunserthe Department of Physical Biochemistry, Max-Planck-Institute of Molecular Physiology, 44227 Dortmund, Germany.
Dietmar J MansteinFrom the Institute for Biophysical Chemistry, Hannover Medical School, OE 4350, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany and.
Medizinische Hochschule Hannover · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular motors of the myosin superfamily share a generic motor domain region. They commonly bind actin in an ATP-sensitive manner, exhibit actin-activated ATPase activity, and generate force and movement in this interaction. Class-18 myosins form heavy chain dimers and contain protein interaction domains located at their unique N-terminal extension. Here, we characterized human myosin-18A molecular function in the interaction with nucleotides, F-actin, and its putative binding partner, the Golgi-associated phosphoprotein GOLPH3. We show that myosin-18A comprises two actin binding sites. One is located in the KE-rich region at the start of the N-terminal extension and appears to mediate ATP-independent binding to F-actin. The second actin-binding site resides in the generic motor domain and is regulated by nucleotide binding in the absence of intrinsic ATP hydrolysis competence. This core motor domain displays its highest actin affinity in the ADP state. Electron micrographs of myosin-18A motor domain-decorated F-actin filaments show a periodic binding pattern independent of the nucleotide state. We show that the PDZ module mediates direct binding of myosin-18A to GOLPH3, and this interaction in turn modulates the actin binding properties of the N-terminal extension. Thus, myosin-18A can act as an actin cross-linker with multiple regulatory modulators that targets interacting proteins or complexes to the actin-based cytoskeleton.

Indexed as

ActinsAdenosine TriphosphateAnimalsBinding SitesCytoskeletonDrosophila melanogasterHumansMembrane ProteinsMiceMyosinsProtein BindingRabbitsRecombinant ProteinsActinsAdenosine TriphosphateGOLPH3 protein, humanMembrane ProteinsMYO18A protein, humanMyosinsRecombinant ProteinsActinCytoskeletonMyosinProtein DomainsProtein-Protein Interactions

Identifiers

PMID23990465
PMCPMC3798472
OpenAlexW2117746386

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.