Evidence map›Paper›PMID 16421248›Full record

ArticleMolecular biology of the cell2006

A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities.

Michael G Clark, Joseph Teply, Brian K Haarer, Susan C Viggiano, David Sept, David C Amberg

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-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

28 citing papers in PubMed, 40 citations in OpenAlex.

  1. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Actin Mechanics and Fragmentation.The Journal of biological chemistry · 2015
    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.

Michael G ClarkDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Joseph Teply
Brian K Haarer
Susan C Viggiano
David Sept
David C Amberg
SUNY Upstate Medical University · USWashington University in St. Louis · US

Funding

Regulation of Actin DynamicsR01GM056189 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI AMBERG, DAVID C · 1998 to 2010
$2.3M
Protein interactions underlying actin-based motilityR01GM067246 · NIGMS · WASHINGTON UNIVERSITY · PI SEPT, DAVID S. · 2002 to 2006
$1.3M
NIGMS NIH HHS GM 067246NIGMS NIH HHS GM 56189NIGMS NIH HHS R01 GM056189NIGMS NIH HHS R01 GM067246
6 · The paper itself

Abstract

Actin interacting protein 1 (Aip1p) and cofilin cooperate to disassemble actin filaments in vitro and are thought to promote rapid turnover of actin networks in vivo. The precise method by which Aip1p participates in these activities has not been defined, although severing and barbed-end capping of actin filaments have been proposed. To better describe the mechanisms and biological consequences of Aip1p activities, we undertook an extensive mutagenesis of AIP1 aimed at disrupting and mapping Aip1p interactions. Site-directed mutagenesis suggested that Aip1p has two actin binding sites, the primary actin binding site lies on the edge of its N-terminal beta-propeller and a secondary actin binding site lies in a comparable location on its C-terminal beta-propeller. Random mutagenesis followed by screening for separation of function mutants led to the identification of several mutants specifically defective for interacting with cofilin but still able to interact with actin. These mutants suggested that cofilin binds across the cleft between the two propeller domains, leaving the actin binding sites exposed and flanking the cofilin binding site. Biochemical, genetic, and cell biological analyses confirmed that the actin binding- and cofilin binding-specific mutants are functionally defective, whereas the genetic analyses further suggested a role for Aip1p in an early, internalization step of endocytosis. A complementary, unbiased molecular modeling approach was used to derive putative structures for the Aip1p-cofilin complex, the most stable of which is completely consistent with the mutagenesis data. We theorize that Aip1p-severing activity may involve simultaneous binding to two actin subunits with cofilin wedged between the two actin binding sites of the N- and C-terminal propeller domains.

Indexed as

Actin CytoskeletonActinsAmino Acid SequenceAmino Acid SubstitutionBinding SitesCofilin 1EndocytosisMicrofilament ProteinsMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein ConformationProtein Interaction MappingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System Techniquesactin interacting protein 1ActinsCOF1 protein, S cerevisiaeCofilin 1Microfilament ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID16421248
PMCPMC1415301
OpenAlexW2165193270

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.