Evidence map›Paper›PMID 19029292›Full record

ArticleThe Journal of biological chemistry2009

MG53 regulates membrane budding and exocytosis in muscle cells.

Chuanxi Cai, Haruko Masumiya, Noah Weisleder, Zui Pan, Miyuki Nishi, Shinji Komazaki, Hiroshi Takeshima, Jianjie Ma

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 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

85 citing papers in PubMed, 125 citations in OpenAlex.

  1. Review
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  10. Is MG53 a potential therapeutic target for cancer?Frontiers in endocrinology · 2023
    Review
  11. Article
  12. Review
  13. Article
  14. Ubiquitin Ligases in Longevity and Aging Skeletal Muscle.International journal of molecular sciences · 2022
    Review
  15. Article
  16. Article
  17. Review
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  19. Review
  20. Article

25 more citing papers are in PubMed but not listed here.

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.

Chuanxi CaiDepartments of Physiology and Biophysics, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Haruko MasumiyaDepartment of Medical Chemistry, Tohoku University Graduate School of Medicine, Miyagi 980-8575, Japan.
Noah WeislederDepartments of Physiology and Biophysics, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Zui PanDepartments of Physiology and Biophysics, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Miyuki NishiDepartment of Medical Chemistry, Tohoku University Graduate School of Medicine, Miyagi 980-8575, Japan; Department of Biological Chemistry, Kyoto University Graduate School of Pharmaceutical Sciences, Kyoto 606-8501, Japan.
Shinji KomazakiDepartment of Anatomy, Saitama Medical University, Saitama 350-0495, Japan.
Hiroshi TakeshimaDepartment of Medical Chemistry, Tohoku University Graduate School of Medicine, Miyagi 980-8575, Japan; Department of Biological Chemistry, Kyoto University Graduate School of Pharmaceutical Sciences, Kyoto 606-8501, Japan. Electronic address: takeshim@pharm.kyoto-u.ac.jp.
Jianjie MaDepartments of Physiology and Biophysics, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854; Department of Medicine, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854. Electronic address: maj2@umdnj.edu.
Johnson University · USKyoto Pharmaceutical University · JPKyoto University · JPSaitama Medical University · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane recycling and remodeling contribute to multiple cellular functions, including cell fusion events during myogenesis. We have identified a tripartite motif (TRIM72) family member protein named MG53 and defined its role in mediating the dynamic process of membrane fusion and exocytosis in striated muscle. MG53 is a muscle-specific protein that contains a TRIM motif at the amino terminus and a SPRY motif at the carboxyl terminus. Live cell imaging of green fluorescent protein-MG53 fusion construct in cultured myoblasts showed that although MG53 contains no transmembrane segment it is tightly associated with intracellular vesicles and sarcolemmal membrane. RNA interference-mediated knockdown of MG53 expression impeded myoblast differentiation, whereas overexpression of MG53 enhanced vesicle trafficking to and budding from sarcolemmal membrane. Co-expression studies indicated that MG53 activity is regulated by a functional interaction with caveolin-3. Our data reveal a new function for TRIM family proteins in regulating membrane trafficking and fusion in striated muscles.

Indexed as

AnimalsBase SequenceCarrier ProteinsCell DifferentiationCell LineCell MembraneCholesterolCricetinaeDNA PrimersExocytosisMembrane ProteinsMiceMicroscopy, ElectronMuscle, SkeletalProtein TransportRNA InterferenceCarrier ProteinsCholesterolDNA PrimersMembrane ProteinsMG53 protein, mouse

Identifiers

PMID19029292
PMCPMC2631961
OpenAlexW2063808790

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.