SMN loss dysregulates microtubule-associated proteins in spinal muscular atrophy model

Özer, Pelin Zobaroğlu; Koyunoğlu, Dila; Son, Çağdaş Devrim; Erdem‐Yurter, Hayat; Bora, Gamze

doi:10.1016/j.mcn.2022.103725

Cited by 3 publications

(2 citation statements)

References 46 publications

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“…MAP 1A combines with and stabilises microtubules by altering the dynamic properties of the cytoskeleton [15]. Under physiological conditions, MAP 1A is responsible for the stability and dynamic regulation of microtubule networks [16]. However, soluble Aβ oligomers can induce MAP 1A degradation in a time‐dependent manner under AD conditions [17].…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of MAP 1A regulates hyperphosphorylation of Tau in Alzheimer's disease model

Cai,

Shao,

et al. 2023

Neuropathology Appl Neurobio

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Background and purposeHyperphosphorylation of Tau is one of the important pathological features of Alzheimer's disease (AD). Therefore, studying the mechanisms behind Tau hyperphosphorylation is crucial in exploring the pathogenesis of neurological damage in AD.MethodsIn this study, after the establishment of rat models of AD, quantitative phosphoproteomics and proteomics were performed to identify proteins, showing that phosphorylation of microtubule associated protein 1A (MAP 1A) was lower in the model group. Western blot confirmed the changes of MAP 1A in the SD rats, APP/PS1 transgenic mice, and cell AD models. To further study the molecular mechanism of recombinant MAP 1A phosphorylation affecting Tau phosphorylation, interfering siRNA‐MAP 1A and protein immunoprecipitation reaction analysis were performed in AD cell models.ResultsCyclin‐dependent kinase 5 (CDK5) showed reduced binding to MAP 1A and increased binding to Tau, resulting in a decrease in phosphorylated MAP 1A (p‐MAP 1A) and an increase in phosphorylated Tau (p‐Tau), and MAP 1A silencing promoted binding of CDK5‐Tau and increased Tau phosphorylation, thereby reducing the cell survival rate.ConclusionsIn summary, we found that p‐MAP 1A downregulation associated with p‐Tau upregulation was due to their altered binding forces to CDK5, and MAP 1A could enhance autophosphorylation by competitive binding to CDK5 and antagonize Tau phosphorylation. This leads to neuronal protection and reducing tissue damage levels in AD, which can help better understand the mechanisms of AD pathogenesis.

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Section: Discussionmentioning

confidence: 99%

Phosphorylation of MAP 1A regulates hyperphosphorylation of Tau in Alzheimer's disease model

Cai,

Shao,

et al. 2023

Neuropathology Appl Neurobio

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“…Microtubule associated proteins (MAPs) are the proteins that interact with cellular cytoskeletal microtubules [36] . Microtubules are primarily stabilized by MAPs, which bind to polymerized or depolymerized tubulin dimers inside the cell [37] .…”

Section: Correlation Analysis Between Daps and Quality Traits Of Filletsmentioning

confidence: 99%

Analysis of quality-related proteins in golden pompano ( Trachinotus ovatus) fillets with modified atmosphere packaging under superchilling storage

Pan,

Zhang,

Chen

et al. 2024

Food Science and Human Wellness

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Here, we aimed to study the changes in proteome of golden pompano fillets during post-mortem storage. Tandem mass tags (TMT) -labeled quantitative proteomic strategy was applied to investigate the relationships between protein changes and quality characteristics of modifi ed atmosphere packaging (MAP) fi llets during superchilling (-3 °C) storage. Scanning electron microscopy was used to show that the muscle histology microstructure of fi llets was damaged to varying degrees, and low-fi eld nuclear magnetic resonance was used to fi nd that the immobilized water and free water in the muscle of fi llets changed signifi cantly. Total sulfhydryl content, TCA-soluble peptides and Ca 2+ -ATPase activity also showed that the fi llet protein had a deterioration by oxidation and denaturation. The Fresh (FS), MAP, and air packaging (AP) groups were set. Total of 150 proteins were identifi ed as differential abundant proteins (DAPs) in MAP/FS, while 209 DAPs were in AP/FS group. The KEGG pathway analysis indicated that most DAPs were involved in binding proteins and protein turnover. Correlation analysis found that 52 DAPs were correlated with quality traits. Among them, 8 highly correlated DAPs are expected to be used as potential quality markers for protein oxidation and water-holding capacity. These results provide a further understanding of the muscle deterioration mechanism of packaging golden pompano fi llets during superchilling.

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More than a marker: potential pathogenic functions of MAP2

DeGiosio

Grubisha

MacDonald

et al. 2022

Front. Mol. Neurosci.

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Microtubule-associated protein 2 (MAP2) is the predominant cytoskeletal regulator within neuronal dendrites, abundant and specific enough to serve as a robust somatodendritic marker. It influences microtubule dynamics and microtubule/actin interactions to control neurite outgrowth and synaptic functions, similarly to the closely related MAP Tau. Though pathology of Tau has been well appreciated in the context of neurodegenerative disorders, the consequences of pathologically dysregulated MAP2 have been little explored, despite alterations in its immunoreactivity, expression, splicing and/or stability being observed in a variety of neurodegenerative and neuropsychiatric disorders including Huntington's disease, prion disease, schizophrenia, autism, major depression and bipolar disorder. Here we review the understood structure and functions of MAP2, including in neurite outgrowth, synaptic plasticity, and regulation of protein folding/transport. We also describe known and potential mechanisms by which MAP2 can be regulated via post-translational modification. Then, we assess existing evidence of its dysregulation in various brain disorders, including from immunohistochemical and (phospho) proteomic data. We propose pathways by which MAP2 pathology could contribute to endophenotypes which characterize these disorders, giving rise to the concept of a "MAP2opathy"-a series of disorders characterized by alterations in MAP2 function.

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SMN loss dysregulates microtubule-associated proteins in spinal muscular atrophy model

Cited by 3 publications

References 46 publications

Phosphorylation of MAP 1A regulates hyperphosphorylation of Tau in Alzheimer's disease model

Phosphorylation of MAP 1A regulates hyperphosphorylation of Tau in Alzheimer's disease model

Analysis of quality-related proteins in golden pompano ( Trachinotus ovatus) fillets with modified atmosphere packaging under superchilling storage

More than a marker: potential pathogenic functions of MAP2

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