Evidence map›Paper›PMID 19633357›Full record

ArticleThe Journal of biological chemistry2009

Bin1 SRC homology 3 domain acts as a scaffold for myofiber sarcomere assembly.

Pasan Fernando, Jacqueline S Sandoz, Wen Ding, Yves de Repentigny, Steve Brunette, John F Kelly, Rashmi Kothary, Lynn A Megeney

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.8field-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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Bend it like BIN1: how a membrane-curving adaptor protein shapes cardiac physiology.American journal of physiology. Heart and circulatory physiology · 2025
    Review
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  3. Article
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  6. Review
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  12. BIN1 regulates dynamic t-tubule membrane.Biochimica et biophysica acta · 2016
    Review
  13. Review
  14. Article
  15. Amphiphysin 2 (BIN1) in physiology and diseases.Journal of molecular medicine (Berlin, Germany) · 2014
    Review
  16. Article
  17. Article
  18. Multilayered regulation of cardiac ion channels.Biochimica et biophysica acta · 2013
    Review
  19. Article
  20. Review
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 5 institutions in 2 countries.

Pasan FernandoThe Sprott Center for Stem Cell Research, Regenerative Medicine Program, Ottawa, Ontario K1H 8L6, Canada. pasan.fernando@mdsinc.com
Jacqueline S Sandoz
Wen Ding
Yves de Repentigny
Steve Brunette
John F Kelly
Rashmi Kothary
Lynn A Megeney
Institute for Biological Sciences · CAInstitute for Stem Cell Biology and Regenerative Medicine · INOttawa Hospital Research InstituteOttawa Hospital · CAStem Cell Network · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In skeletal muscle development, the genes and regulatory factors that govern the specification of myocytes are well described. Despite this knowledge, the mechanisms that regulate the coordinated assembly of myofiber proteins into the functional contractile unit or sarcomere remain undefined. Here we explored the hypothesis that modular domain proteins such as Bin1 coordinate protein interactions to promote sarcomere formation. We demonstrate that Bin1 facilitates sarcomere organization through protein-protein interactions as mediated by the Src homology 3 (SH3) domain. We observed a profound disorder in myofiber size and structural organization in a murine model expressing the Bin1 SH3 region. In addition, satellite cell-derived myogenesis was limited despite the accumulation of skeletal muscle-specific proteins. Our experiments revealed that the Bin1 SH3 domain formed transient protein complexes with both actin and myosin filaments and the pro-myogenic kinase Cdk5. Bin1 also associated with a Cdk5 phosphorylation domain of titin. Collectively, these observations suggest that Bin1 displays protein scaffold-like properties and binds with sarcomeric factors important in directing sarcomere protein assembly and myofiber maturation.

Indexed as

src Homology DomainsAdaptor Proteins, Signal TransducingAnimalsCell DifferentiationCell LineGene Expression Regulation, DevelopmentalMiceMice, TransgenicMuscle Fibers, SkeletalNerve Tissue ProteinsPhenotypeSarcomeresTumor Suppressor ProteinsAdaptor Proteins, Signal TransducingBin1 protein, mouseNerve Tissue ProteinsTumor Suppressor Proteins

Identifiers

PMID19633357
PMCPMC2785696
OpenAlexW2019507798

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.