Evidence map›Paper›PMID 21246116›Full record

ArticleMolecular bioSystems2011

Identification of an FHL1 protein complex containing ACTN1, ACTN4, and PDLIM1 using affinity purifications and MS-based protein-protein interaction analysis.

Parveen Sharma, Thiruchelvi Shathasivam, Vladimir Ignatchenko, Thomas Kislinger, Anthony O Gramolini

Open access · greenAbstract read
In one paragraph

Article in Molecular bioSystems, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.9field-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

20 citing papers in PubMed, 30 citations in OpenAlex.

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  6. The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022
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  15. Design and formulation of functional pluripotent stem cell-derived cardiac microtissues.Proceedings of the National Academy of Sciences of the United States of America · 2013
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  18. α-Crystallin B prevents apoptosis after H2O2 exposure in mouse neonatal cardiomyocytes.American journal of physiology. Heart and circulatory physiology · 2012
    Article
  19. Article
  20. 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.

Parveen SharmaDepartment of Physiology, University of Toronto, Toronto, Ontario, Canada.
Thiruchelvi Shathasivam
Vladimir Ignatchenko
Thomas Kislinger
Anthony O Gramolini
University of Toronto · CAOntario Institute for Cancer Research · CA

Funding

CIHR 87143-1CIHR MOP-84267
6 · The paper itself

Abstract

introductionFour and a half LIM domains protein 1 (FHL1) is the most widely expressed member of the FHL family of proteins, consisting of four and a half highly conserved LIM domains. A multifunctional and integral role for FHL1 has been implicated in muscle development, structural maintenance, and signaling. To date, 27 FHL1 mutations have been identified that result in at least six different X-linked myopathies, with patients often presenting with cardiovascular complications. Since proteins assemble into dynamic complexes within the cell, FHL1 likely mediates its biological functions in conjunction with other proteins. Delineation of FHL1 interactions could provide insight into its regulatory functions.

methodsWe performed tandem affinity purification from human embryonic kidney 293 (HEK-293) cells to purify FHL1 and interacting proteins. To identify the potential interactors of FHL1 we performed a total of 9 different purifications from HEK-293 cells which included 3 experimental replicates for each biological condition: FHL1, tag control (DPYSL3), and negative control (empty vector). Purified samples were analyzed by liquid chromatography mass spectrometry (LC-MS). Potential interactors were then verified by immunoprecipitation from mouse heart ventricles and interactions visualized in adult cardiomyocytes using 3D fluorescence microscopy.

resultsWe identified a total of 310 different proteins from all 9 purifications and by applying stringent filtering criteria we eliminated all proteins found in any of the controls and only allowed those that were detected in two or more bait purification. We identified 34 high confidence potential binding partners of FHL1. We then showed that FHL1 exists as part of a complex that binds with PDLIM1, GSN and ACTN1.

Indexed as

ActininChromatography, AffinityIntracellular Signaling Peptides and ProteinsMass SpectrometryMicrofilament ProteinsMuscle ProteinsAnimalsComputational BiologyGelsolinHEK293 CellsHumansLIM Domain ProteinsMiceProtein BindingRecombinant Fusion ProteinsTranscription FactorsActininACTN1 protein, humanACTN4 protein, humanFHL1 protein, humanGelsolinIntracellular Signaling Peptides and ProteinsLDB2 protein, humanLIM Domain ProteinsMicrofilament ProteinsMuscle ProteinsRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID21246116
PMCPMC3711787
OpenAlexW2127526666

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.