Evidence map›Paper›PMID 19298826›Full record

ArticleJournal of molecular biology2009

Nucleotide- and activator-dependent structural and dynamic changes of arp2/3 complex monitored by hydrogen/deuterium exchange and mass spectrometry.

Wendy D Zencheck, Hui Xiao, Brad J Nolen, Ruth Hogue Angeletti, Thomas D Pollard, Steven C Almo

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification of Wiskott-Aldrich syndrome protein (WASP) binding sites on the branched actin filament nucleator Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Review
  5. Review
  6. Article
  7. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  8. Article
  9. A nucleator arms race: cellular control of actin assembly.Nature reviews. Molecular cell biology · 2010
    Review
  10. Article
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 4 institutions in 1 country.

Wendy D ZencheckDepartment of Biochemistry, Yeshiva University, Bronx, NY 10461, USA.
Hui Xiao
Brad J Nolen
Ruth Hogue Angeletti
Thomas D Pollard
Steven C Almo
Albert Einstein College of Medicine · USUniversity of Oregon · USYale University · USYeshiva University · US

Funding

Structure and function of Arp 2/3 complex--Subproject 4P01GM066311 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 2003 to 2013
$16.8M
MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008572 · NIGMS · YESHIVA UNIVERSITY · PI BRENOWITZ, MICHAEL D. · 1995 to 2009
$3.0M
FT-ICR MASS SPECTROMETER: TYPE 1 DIABETESS10RR019891 · NCRR · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI ANGELETTI, RUTH HOGUE · 2004 to 2004
$1.7M
MASS SPECTROMETER SYSTEM: OBESITYS10RR019352 · NCRR · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI ANGELETTI, RUTH HOGUE · 2004 to 2004
$379k
Structural investigation of Arp2/3 complex activationF32GM074374 · NIGMS · YALE UNIVERSITY · PI NOLEN, BRADLEY J. · 2005 to 2006
$93k
NCRR NIH HHS S10 RR019352NCRR NIH HHS S10 RR019891NIGMS NIH HHS F32 GM074374NIGMS NIH HHS GM008572NIGMS NIH HHS GM066311NIGMS NIH HHS P01 GM066311NIGMS NIH HHS T32 GM008572
6 · The paper itself

Abstract

Arp2/3 complex plays a central role in the de novo nucleation of filamentous actin as branches on existing filaments. The complex must bind ATP, protein activators [e.g., Wiskott-Aldrich syndrome protein (WASp)], and the side of an actin filament to form a new actin filament. Amide hydrogen/deuterium exchange coupled with mass spectrometry was used to examine the structural and dynamic properties of the mammalian Arp2/3 complex in the presence of both ATP and the activating peptide segment from WASp. Changes in the rate of hydrogen exchange indicate that ATP binding causes conformational rearrangements of Arp2 and Arp3 that are transmitted allosterically to the Arp complex (ARPC)1, ARPC2, ARPC4, and ARPC5 subunits. These data are consistent with the closure of nucleotide-binding cleft of Arp3 upon ATP binding, resulting in structural rearrangements that propagate throughout the complex. Binding of the VCA domain of WASp to ATP-Arp2/3 further modulates the rates of hydrogen exchange in these subunits, indicating that a global conformational reorganization is occurring. These effects may include the direct binding of activators to Arp3, Arp2, and ARPC1; alterations in the relative orientations of Arp2 and Arp3; and the long-range transmission of activator-dependent signals to segments proposed to be involved in binding the F-actin mother filament.

Indexed as

Protein Structure, QuaternaryActin CytoskeletonActin-Related Protein 2-3 ComplexAdenosine TriphosphateAllosteric RegulationAnimalsCattleModels, MolecularThymus GlandWiskott-Aldrich Syndrome ProteinActin-Related Protein 2-3 ComplexAdenosine TriphosphateWiskott-Aldrich Syndrome Protein

Identifiers

PMID19298826
PMCPMC2983480
OpenAlexW1986559412

What OpenQuestion holds

Textmetadata
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.