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Cited by 26Genetics and Neurodevelopmental DisordersLipid Membrane Structure and BehaviorAutism Spectrum Disorder Research

Quantitative Profiling of Brain Lipid Raft Proteome in a Mouse Model of Fragile X Syndrome

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Kalinowska, Magdalena, Castillo, Catherine, Francesconi, Anna·2015·PLOS ONE
DOI 10.1371/journal.pone.0121464PMC PMC4388542
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Abstract

Fragile X Syndrome, a leading cause of inherited intellectual disability and autism, arises from transcriptional silencing of the FMR1 gene encoding an RNA-binding protein, Fragile X Mental Retardation Protein (FMRP). FMRP can regulate the expression of approximately 4% of brain transcripts through its role in regulation of mRNA transport, stability and translation, thus providing a molecular rationale for its potential pleiotropic effects on neuronal and brain circuitry function. Several intracellular signaling pathways are dysregulated in the absence of FMRP suggesting that cellular deficits may be broad and could result in homeostatic changes. Lipid rafts are specialized regions of the plasma membrane, enriched in cholesterol and glycosphingolipids, involved in regulation of intracellular signaling. Among transcripts targeted by FMRP, a subset encodes proteins involved in lipid biosynthesis and homeostasis, dysregulation of which could affect the integrity and function of lipid rafts. Using a quantitative mass spectrometry-based approach we analyzed the lipid raft proteome of Fmr1 knockout mice, an animal model of Fragile X syndrome, and identified candidate proteins that are differentially represented in Fmr1 knockout mice lipid rafts. Furthermore, network analysis of these candidate proteins reveals connectivity between them and predicts functional connectivity with genes encoding components of myelin sheath, axonal processes and growth cones. Our findings provide insight to aid identification of molecular and cellular dysfunctions arising from Fmr1 silencing and for uncovering shared pathologies between Fragile X syndrome and other autism spectrum disorders.

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Authors
Kalinowska, M., Castillo, C., & Francesconi, A.
Affiliations
Albert Einstein College of Medicine (US)
Corresponding author
Francesconi, Anna
ORCID
Venue
PLOS ONE
Publisher
Public Library of Science (PLoS)
Published
2015-04-07
Volume
10
Issue
4
Pages
e0121464
ISSN
1932-6203 (ISSN-L)
DOI
10.1371/journal.pone.0121464
PMC
PMC4388542
OpenAlex
W2000186718
Cited by
26
References
12
Citations by year
2026: 1 · 2025: 2 · 2024: 3 · 2023: 3 · 2022: 4 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 3 · 2016: 4 · 2015: 1
FWCI
2.06
Type
journal article
Language
en
Open access
Licence
Locations
  • PLoS ONE (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Figshare (submittedVersion, cc-by)
Funders
  • Autism Speaks
  • National Institutes of Health
  • U.S. Public Health Service
  • National Institute of Mental Health (MH082870, R01MH082870)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Neuroscience › Cognitive Neuroscience › Autism Spectrum Disorder Research
Keywords
fragile X syndrome, lipid rafts, FMRP, Fmr1 knockout mice, lipogenesis, cholesterol, glycosphingolipids, myelin sheath, axonal processes, growth cones, autism spectrum disorder, intellectual disability, protein network analysis
MeSH terms
Animals, Brain, Disease Models, Animal, Fragile X Syndrome, Humans, Membrane Proteins, Mice, Knockout, Proteome, Membrane Microdomains, Mice, Fragile X Mental Retardation Protein, Fragile X Messenger Ribonucleoprotein 1

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