Evidence map›Paper›PMID 17597155›Full record

ArticleJournal of molecular biology2007

Evidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins.

Susan Lowey, Lakshmi D Saraswat, HongJun Liu, Niels Volkmann, Dorit Hanein

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

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  15. Alternative N-terminal regions ofThe Journal of biological chemistry · 2020
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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

5 authors at 2 institutions in 1 country.

Susan LoweyDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA. lowey@physiology.med.uvm.edu
Lakshmi D Saraswat
HongJun Liu
Niels Volkmann
Dorit Hanein
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of Vermont · US

Funding

Structural/biochemical analysis of myosin based movementP01AR047906 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 2001 to 2005
$6.5M
Structure Comparison Of Strongly bound Actomyosin StatesR01AR047199 · NIAMS · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI HANEIN, DORIT · 2001 to 2005
$1.9M
Automated docking and modeling for electron microscopyR01GM076503 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI VOLKMANN, NIELS · 2006 to 2010
$1.4M
NIAMS NIH HHS AR47199NIAMS NIH HHS AR47906NIAMS NIH HHS P01 AR047906NIAMS NIH HHS R01 AR047199NIGMS NIH HHS GM076503NIGMS NIH HHS R01 GM076503
6 · The paper itself

Abstract

The function of the src-homology 3 (SH3) domain in class II myosins, a distinct beta-barrel structure, remains unknown. Here, we provide evidence, using electron cryomicroscopy, in conjunction with light-scattering, fluorescence and kinetic analyses, that the SH3 domain facilitates the binding of the N-terminal extension of the essential light chain isoform (ELC-1) to actin. The 41 residue extension contains four conserved lysine residues followed by a repeating sequence of seven Pro/Ala residues. It is widely believed that the highly charged region interacts with actin, while the Pro/Ala-rich sequence forms a rigid tether that bridges the approximately 9 nm distance between the myosin lever arm and the thin filament. In order to localize the N terminus of ELC in the actomyosin complex, an engineered Cys was reacted with undecagold-maleimide, and the labeled ELC was exchanged into myosin subfragment-1 (S1). Electron cryomicroscopy of S1-bound actin filaments, together with computer-based docking of the skeletal S1 crystal structure into 3D reconstructions, showed a well-defined peak for the gold cluster near the SH3 domain. Given that SH3 domains are known to bind proline-rich ligands, we suggest that the N-terminal extension of ELC interacts with actin and modulates myosin kinetics by binding to the SH3 domain during the ATPase cycle.

Indexed as

Amino Acid SequenceAnimalsChickensCryoelectron MicroscopyFluorescence Resonance Energy TransferModels, MolecularMolecular Sequence DataMyosinsProtein IsoformsSequence Alignmentsrc Homology DomainsMyosinsProtein Isoforms

Identifiers

PMID17597155
PMCPMC2693010
OpenAlexW2052478550

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.