Evidence map›Paper›PMID 15872087›Full record

ArticleMolecular biology of the cell2005

Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions.

Omar Quintero-Monzon, Avital A Rodal, Boris Strokopytov, Steven C Almo, Bruce L Goode

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Drebrin-induced stabilization of actin filaments.The Journal of biological chemistry · 2013
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. NMR solution structures of actin depolymerizing factor homology domains.Protein science : a publication of the Protein Society · 2009
    Article
  14. Article
  15. Article
  16. Structural basis and evolutionary origin of actin filament capping by twinfilin.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  18. 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

5 authors at 2 institutions in 1 country.

Omar Quintero-MonzonDepartment of Biology and Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA. goode@brandeis.edu
Avital A Rodal
Boris Strokopytov
Steven C Almo
Bruce L Goode
Brandeis University · USAlbert Einstein College of Medicine · US

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
Macromolecular Structure MechanismT32GM007596 · NIGMS · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1985 to 2019
$4.5M
STRUCTURAL BIOLOGY OF CYTOSKELETAL DYNAMICSR01GM053807 · NIGMS · YESHIVA UNIVERSITY · PI ALMO, STEVEN C. · 1995 to 2003
$1.3M
NIGMS NIH HHS GM-53807NIGMS NIH HHS GM-63691NIGMS NIH HHS R01 GM053807NIGMS NIH HHS R01 GM063691NIGMS NIH HHS T32 GM007596
6 · The paper itself

Abstract

Abp1 is a multidomain protein that regulates the Arp2/3 complex and links proteins involved in endocytosis to the actin cytoskeleton. All of the proposed cellular functions of Abp1 involve actin filament binding, yet the actin binding site(s) on Abp1 have not been identified, nor has the importance of actin binding for Abp1 localization and function in vivo been tested. Here, we report the crystal structure of the Saccharomyces cerevisiae Abp1 actin-binding actin depolymerizing factor homology (ADFH) domain and dissect its activities by mutagenesis. Abp1-ADFH domain and ADF/cofilin structures are similar, and they use conserved surfaces to bind actin; however, there are also key differences that help explain their differential effects on actin dynamics. Using point mutations, we demonstrate that actin binding is required for localization of Abp1 in vivo, the lethality caused by Abp1 overexpression, and the ability of Abp1 to activate Arp2/3 complex. Furthermore, we genetically uncouple ABP1 functions that overlap with SAC6, SLA1, and SLA2, showing they require distinct combinations of activities and interactions. Together, our data provide the first structural and functional view of the Abp1-actin interaction and show that Abp1 has distinct cellular roles as an adapter, linking different sets of ligands for each function.

Indexed as

ActinsAllelesAmino Acid SequenceBinding SitesCrystallography, X-RayEndocytosisGreen Fluorescent ProteinsImmunoblottingKineticsLigandsMicrofilament ProteinsMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataMutagenesisMutationABP1 protein, S cerevisiaeActinsGreen Fluorescent ProteinsLigandsMicrofilament ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID15872087
PMCPMC1165398
OpenAlexW2155470250

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.