Tau Toxicity in Neurodegeneration

Liang, Shuyu; Wang, Zuo-Teng; Tan, Lan; Yu, Jin‐Tai

doi:10.1007/s12035-022-02809-3

Cited by 19 publications

(9 citation statements)

References 145 publications

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“…Tau was first described as a natively unfolded microtubule-associated protein. In fact, its main function is to promote the assembly of microtubules and stabilize their structure [ 13 ]. However, Tau proteins have a variety of other functions, which include maintaining the structural integrity of neurons, contributing to signal transmission between neurons, and axonal transport [ 1 , 13 ].…”

Section: Tau Isoformsmentioning

confidence: 99%

“…In fact, its main function is to promote the assembly of microtubules and stabilize their structure [ 13 ]. However, Tau proteins have a variety of other functions, which include maintaining the structural integrity of neurons, contributing to signal transmission between neurons, and axonal transport [ 1 , 13 ]. Tau also plays a role in regulating myelination, iron homeostasis, and neurogenesis [ 13 ] and may also support synaptic plasticity [ 52 ].…”

Section: Tau Isoformsmentioning

confidence: 99%

“…Furthermore, Tau aggregation has been found in the muscles of patients diagnosed with inclusion body myositis (IBM) [ 10 , 11 ]. Additional roles other than mediating microtubule polymerization and stabilization have been attributed to Tau, including regulation of signal transduction and axonal transport, protecting genomic architecture, RNA metabolism, and protein synthesis [ 12 , 13 ].…”

Section: Introductionmentioning

confidence: 99%

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Tau Isoforms: Gaining Insight into MAPT Alternative Splicing

Corsi

Bombieri

Valenti

2022

IJMS

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Tau microtubule-associated proteins, encoded by the MAPT gene, are mainly expressed in neurons participating in axonal transport and synaptic plasticity. Six major isoforms differentially expressed during cell development and differentiation are translated by alternative splicing of MAPT transcripts. Alterations in the expression of human Tau isoforms and their aggregation have been linked to several neurodegenerative diseases called tauopathies, including Alzheimer’s disease, progressive supranuclear palsy, Pick’s disease, and frontotemporal dementia with parkinsonism linked to chromosome 17. Great efforts have been dedicated in recent years to shed light on the complex regulatory mechanism of Tau splicing, with a perspective to developing new RNA-based therapies. This review summarizes the most recent contributions to the knowledge of Tau isoform expression and experimental models, highlighting the role of cis-elements and ribonucleoproteins that regulate the alternative splicing of Tau exons.

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Section: Tau Isoformsmentioning

confidence: 99%

Section: Tau Isoformsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Tau Isoforms: Gaining Insight into MAPT Alternative Splicing

Corsi

Bombieri

Valenti

2022

IJMS

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“…According to current epidemiological data, the global prevalence of AD will increase three folds by 2050. Current research on the pathogenesis of AD has generated a number of pathophysiological hypotheses that include amyloid-beta (Aβ) toxicity (Selkoe and Hardy, 2016), tau protein hyperphosphorylation (Liang et al, 2022), and synaptic dysfunction (Skaper et al, 2017). Optogenetics provides a novel approach to the study of AD pathogenesis and its clinical treatment.…”

Section: Alzheimer's Diseasementioning

confidence: 99%

Applications and challenges of rhodopsin-based optogenetics in biomedicine

et al. 2022

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Optogenetics is an emerging bioengineering technology that has been rapidly developed in recent years by cross-integrating optics, genetic engineering, electrophysiology, software control, and other disciplines. Since the first demonstration of the millisecond neuromodulation ability of the channelrhodopsin-2 (ChR2), the application of optogenetic technology in basic life science research has been rapidly progressed, especially in neurobiology, which has driven the development of the discipline. As the optogenetic tool protein, microbial rhodopsins have been continuously explored, modified, and optimized, with many variants becoming available, with structural characteristics and functions that are highly diversified. Their applicability has been broadened, encouraging more researchers and clinicians to utilize optogenetics technology in research. In this review, we summarize the species and variant types of the most important class of tool proteins in optogenetic techniques, the microbial rhodopsins, and review the current applications of optogenetics based on rhodopsin qualitative light in biology and other fields. We also review the challenges facing this technology, to ultimately provide an in-depth technical reference to support the application of optogenetics in translational and clinical research.

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“…It appears that dysfunctions of the tau protein might play the crucial role there. This protein is normally associated with microtubules and promotes their assembly, as well as stabilizes these structures (physiological roles of tau have been reviewed recently by Liang et al 2022). Due to alternative splicing of mRNA of the tau-encoding gene (the MAPT gene), there are 6 isoforms of the tau protein which differ in the length, ranging from 352 to 441 amino acid residues.…”

Section: Alzheimer's Diseasementioning

confidence: 99%

Tubulin Cytoskeleton in Neurodegenerative Diseases–not Only Primary Tubulinopathies

et al. 2022

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Neurodegenerative diseases represent a large group of disorders characterized by gradual loss of neurons and functions of the central nervous systems. Their course is usually severe, leading to high morbidity and subsequent inability of patients to independent functioning. Vast majority of neurodegenerative diseases is currently untreatable, and only some symptomatic drugs are available which efficacy is usually very limited. To develop novel therapies for this group of diseases, it is crucial to understand their pathogenesis and to recognize factors which can influence the disease course. One of cellular structures which dysfunction appears to be relatively poorly understood in the light of neurodegenerative diseases is tubulin cytoskeleton. On the other hand, its changes, both structural and functional, can considerably influence cell physiology, leading to pathological processes occurring also in neurons. In this review, we summarize and discuss dysfunctions of tubulin cytoskeleton in various neurodegenerative diseases different than primary tubulinopathies (caused by mutations in genes encoding the components of the tubulin cytoskeleton), especially Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, amyotrophic lateral sclerosis, prion diseases, and neuronopathic mucopolysaccharidoses. It is also proposed that correction of these disorders might attenuate the progress of specific diseases, thus, finding newly recognized molecular targets for potential drugs might become possible.

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Tau Toxicity in Neurodegeneration

Cited by 19 publications

References 145 publications

Tau Isoforms: Gaining Insight into MAPT Alternative Splicing

Tau Isoforms: Gaining Insight into MAPT Alternative Splicing

Applications and challenges of rhodopsin-based optogenetics in biomedicine

Tubulin Cytoskeleton in Neurodegenerative Diseases–not Only Primary Tubulinopathies

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