Evidence map›Paper›PMID 22334701›Full record

ArticleThe Journal of biological chemistry2012

Alix protein is substrate of Ozz-E3 ligase and modulates actin remodeling in skeletal muscle.

Antonella Bongiovanni, Daniele P Romancino, Yvan Campos, Gaetano Paterniti, Xiaohui Qiu, Simon Moshiach, Valentina Di Felice, Naja Vergani, Duran Ustek, Alessandra d'Azzo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Relaxin-2: Shaping the Proteomic Landscape of Skeletal Muscle Physiology, Glucose Trafficking, and Mitochondrial Function in Rat.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Mitochondrial proteostasis regulated by CRL5Communications biology · 2025
    Article
  3. Shining a Light on Skeletal Muscle Regeneration: Red Photobiomodulation Boosts Myoblast Differentiation In Vitro.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
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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

10 authors at 4 institutions in 2 countries.

Antonella BongiovanniInstitute of Biomedicine and Molecular Immunology, National Research Council, 90146 Palermo, Italy. bongiovanni@ibim.cnr.it
Daniele P Romancino
Yvan Campos
Gaetano Paterniti
Xiaohui Qiu
Simon Moshiach
Valentina Di Felice
Naja Vergani
Duran Ustek
Alessandra d'Azzo
St. Jude Children's Research Hospital · USNational Research Council · ITIstituto di Biomedicina e di Immunologia Molecolare Alberto Monroy · ITUniversity of Palermo · IT

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Specificity and Activity of Ozz-E3 During MyogenesisR01AR049867 · NIAMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI D'AZZO, ALESSANDRA · 2004 to 2008
$1.2M
NCI NIH HHS CA021765NCI NIH HHS P30 CA021765NIAMS NIH HHS AR049867NIAMS NIH HHS R01 AR049867
6 · The paper itself

Abstract

Alix/AIP1 is a multifunctional adaptor protein that participates in basic cellular processes, including membrane trafficking and actin cytoskeleton assembly, by binding selectively to a variety of partner proteins. However, the mechanisms regulating Alix turnover, subcellular distribution, and function in muscle cells are unknown. We now report that Alix is expressed in skeletal muscle throughout myogenic differentiation. In myotubes, a specific pool of Alix colocalizes with Ozz, the substrate-binding component of the muscle-specific ubiquitin ligase complex Ozz-E3. We found that interaction of the two endogenous proteins in the differentiated muscle fibers changes Alix conformation and promotes its ubiquitination. This in turn regulates the levels of the protein in specific subcompartments, in particular the one containing the actin polymerization factor cortactin. In Ozz(-/-) myotubes, the levels of filamentous (F)-actin is perturbed, and Alix accumulates in large puncta positive for cortactin. In line with this observation, we show that the knockdown of Alix expression in C2C12 muscle cells affects the amount and distribution of F-actin, which consequently leads to changes in cell morphology, impaired formation of sarcolemmal protrusions, and defective cell motility. These findings suggest that the Ozz-E3 ligase regulates Alix at sites where the actin cytoskeleton undergoes remodeling.

Indexed as

Actin CytoskeletonAnimalsCalcium-Binding ProteinsCell AdhesionCell LineCell MovementCortactinMiceMice, KnockoutMuscle Fibers, SkeletalMuscle, SkeletalProtein BindingProtein Interaction Domains and MotifsProtein TransportPseudopodiaRepressor ProteinsCalcium-Binding ProteinsCortactinNeurl2 protein, mousePdcd6ip protein, mouseRepressor ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID22334701
PMCPMC3320967
OpenAlexW1988994171

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.