Evidence map›Paper›PMID 20886612›Full record

ArticleCytoskeleton (Hoboken, N.J.)2010

Arg/Abl-binding protein, a Z-body and Z-band protein, binds sarcomeric, costameric, and signaling molecules.

Jean M Sanger, Jushuo Wang, Lisa M Gleason, Prokash Chowrashi, Dipak K Dube, Balraj Mittal, Victoria Zhukareva, Joseph W Sanger

Open access · bronzeAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Impact of Sorbs2 dysfunction on cardiovascular diseases.Biochimica et biophysica acta. Molecular basis of disease · 2025
    Review
  3. Article
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  8. eLife · 2021
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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

8 authors at 3 institutions in 2 countries.

Jean M SangerDepartment of Cell and Developmental Biology, SUNY Upstate Medical University, Syracuse, New York 13210, USA. sangerjm@upstate.edu
Jushuo Wang
Lisa M Gleason
Prokash Chowrashi
Dipak K Dube
Balraj Mittal
Victoria Zhukareva
Joseph W Sanger
SUNY Upstate Medical University · USSanjay Gandhi Post Graduate Institute of Medical Sciences · INUniversity of Pennsylvania · US

Funding

Analysis of Z-band assembly and maintenance in living skeletal muscle cellsR01AR057063 · NIAMS · UPSTATE MEDICAL UNIVERSITY · PI SANGER, JEAN M, SANGER, JOSEPH WILLIAM · 2009 to 2013
$1.7M
Dynamics of Proteins in the A-bands of Cardiac MuscleR01HL080426 · NHLBI · UPSTATE MEDICAL UNIVERSITY · PI SANGER, JOSEPH WILLIAM · 2006 to 2009
$1.4M
NHLBI NIH HHS R01 HL080426NIAMS NIH HHS R01 AR057063
6 · The paper itself

Abstract

ArgBP2 (Arg/Abl-Binding Protein) is expressed at high levels in the heart and is localized in the Z-bands of mature myofibrils. ArgBP2 is a member of a small family of proteins that also includes vinexin and CAP (c-Cbl-associated protein), all characterized by having one sorbin homology (SOHO) domain and three C-terminal SH3 domains. Antibodies directed against ArgBP2 also react with the Z-bodies of myofibril precursors: premyofibrils and nascent myofibrils. Expression in cardiomyocytes of plasmids encoding Yellow Fluorescent Protein (YFP) fused to either full length ArgBP2, the SOHO, mid-ArgBP or the SH3 domains of ArgBP2 led to Z-band targeting of the fusion proteins, whereas an N-terminal fragment lacking these domains did not target to Z-bands. Although ArgBP2 is not found in skeletal muscle cells, YFP-ArgBP2 did target to Z-bodies and Z-bands in cultured myotubes. GST-ArgBP2-SH3 bound actin, α-actinin and vinculin proteins in blot overlays, cosedimentation assays, and EM negative staining techniques. Over-expression of ArgBP2 and ArgBP2-SH3 domains, but not YFP alone, led to loss of myofibrils in cardiomyocytes. Fluorescence recovery after photobleaching was used to measure the rapid dynamics of both the full length and some truncated versions of ArgBP2. Our results indicate that ArgBP2 may play an important role in the assembly and maintenance of myofibrils in cardiomyocytes.

Indexed as

ActinsAdaptor Proteins, Signal TransducingAnimalsChick EmbryoCytoskeletal ProteinsHomeodomain ProteinsHumansMuscle Fibers, SkeletalMuscle ProteinsMuscle, SkeletalMyocytes, CardiacMyofibrilsProtein BindingQuailRNA-Binding ProteinsSarcomeresActinsAdaptor Proteins, Signal TransducingCytoskeletal ProteinsHomeodomain ProteinsMuscle ProteinsRNA-Binding ProteinsSORBS2 protein, humanVinculin

Identifiers

PMID20886612
PMCPMC3019100
OpenAlexW1977200592

What OpenQuestion holds

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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.