Binding of Microtubule Proteins to DNA: Specificity of the Interaction

Corcés, Victor G.; Salas, José Valero; Salas, María; Ávila, Jesús

doi:10.1111/j.1432-1033.1978.tb12330.x

Cited by 46 publications

(15 citation statements)

References 36 publications

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“…Considering the relationship between the DNA and RNA, this finding also suggested a possible interaction between tau and the DNA. Indeed, Corces et al showed that brain depolymerised microtubule-associated proteins bind the DNA with high affinity [ 70 ]. Using an in vitro assay, Corces et al further showed that DNA inhibits microtubule assembly in a concentration-dependent manner, indicating that microtubule-associated proteins have more affinity to the DNA than to the microtubules [ 71 ].…”

Section: Nuclear Tau and Alzheimer’s Diseasementioning

confidence: 99%

“…The capacity of tau to interact with nucleic acids, such as the RNA and DNA [ 68 , 69 , 70 , 71 ], and raise the melting temperature of the DNA suggests it could also play a role in DNA protection [ 72 ] ( Figure 3 ). In vitro evidence showed that tau could protect the dsDNA from thermal denaturation and enhance its renaturation [ 78 ].…”

Section: Nuclear Tau and Alzheimer’s Diseasementioning

confidence: 99%

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Nuclear Tau and Its Potential Role in Alzheimer’s Disease

2016

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Tau protein, found in both neuronal and non-neuronal cells, forms aggregates in neurons that constitutes one of the hallmarks of Alzheimer’s disease (AD). For nearly four decades, research efforts have focused more on tau’s role in physiology and pathology in the context of the microtubules, even though, for over three decades, tau has been localised in the nucleus and the nucleolus. Its nuclear and nucleolar localisation had stimulated many questions regarding its role in these compartments. Data from cell culture, mouse brain, and the human brain suggests that nuclear tau could be essential for genome defense against cellular distress. However, its nature of translocation to the nucleus, its nuclear conformation and interaction with the DNA and other nuclear proteins highly suggest it could play multiple roles in the nucleus. To find efficient tau-based therapies, there is a need to understand more about the functional relevance of the varied cellular distribution of tau, identify whether specific tau transcripts or isoforms could predict tau’s localisation and function and how they are altered in diseases like AD. Here, we explore the cellular distribution of tau, its nuclear localisation and function and its possible involvement in neurodegeneration.

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Section: Nuclear Tau and Alzheimer’s Diseasementioning

confidence: 99%

Section: Nuclear Tau and Alzheimer’s Diseasementioning

confidence: 99%

Nuclear Tau and Its Potential Role in Alzheimer’s Disease

2016

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“…Although Tau protein hyperphosphorylation and aggregation are hallmarks associated with the progress of the disease [16], recent studies point to a nuclear origin of AD, whereby nuclear Tau [17,18], and NL proteins [19,20] would play a decisive role. Tau interacts with DNA [21][22][23], including heterochromatin contacts [24,25], genome protection [26][27][28][29] by modulating euchromatin gene expression [30,31] and it accumulates in cell nuclei throughout neuronal aging [32]. AD onset and progression takes place in parallel with the gradual disappearance of Tau from neuronal nuclei and its accumulation in the cytoplasm [17].…”

Section: Introductionmentioning

confidence: 99%

Perinuclear Lamin A and Nucleoplasmic Lamin B2 Characterize Two Types of Hippocampal Neurons through Alzheimer’s Disease Progression

Gil

Niño

Chi‐Ahumada

et al. 2020

IJMS

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Background. Recent reports point to a nuclear origin of Alzheimer’s disease (AD). Aged postmitotic neurons try to repair their damaged DNA by entering the cell cycle. This aberrant cell cycle re-entry involves chromatin modifications where nuclear Tau and the nuclear lamin are involved. The purpose of this work was to elucidate their participation in the nuclear pathological transformation of neurons at early AD. Methodology. The study was performed in hippocampal paraffin embedded sections of adult, senile, and AD brains at I-VI Braak stages. We analyzed phospho-Tau, lamins A, B1, B2, and C, nucleophosmin (B23) and the epigenetic marker H4K20me3 by immunohistochemistry. Results. Two neuronal populations were found across AD stages, one is characterized by a significant increase of Lamin A expression, reinforced perinuclear Lamin B2, elevated expression of H4K20me3 and nuclear Tau loss, while neurons with nucleoplasmic Lamin B2 constitute a second population. Conclusions. The abnormal cell cycle reentry in early AD implies a fundamental neuronal transformation. This implies the reorganization of the nucleo-cytoskeleton through the expression of the highly regulated Lamin A, heterochromatin repression and building of toxic neuronal tangles. This work demonstrates that nuclear Tau and lamin modifications in hippocampal neurons are crucial events in age-related neurodegeneration.

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“…Since DNA binds to MAPs, but not to tubulin [26], we suggest that the presence of MAPS facilitates the zinc-tubulin oligomers formation. Depletion of MAPS results in longer and wider tubulin-sheets.…”

Section: Influence Of Maps In Length and Width Of Sheetsmentioning

confidence: 94%

Factors implicated in determining the structure of zinc tubulin‐sheets: Lateral tubulin–tubulin interaction is promoted by the presence of zinc

Torre

Villasanté

Corral

et al. 1981

J. Supramol. Struct. Cell. Biochem.

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Addition of increasing amounts of zinc to a cold microtubule protein solution results in the disappearance of 30 S oligomer found in the absence of that cation and in the appearance of new tubulin oligomers, 90 S and 23 S. When a microtubule protein solution is warmed in the presence of zinc, tubulin-sheets are assembled. We have tested the influence of microtubule associated proteins and the zinc:tubulin ratio on the polymerization process. Depletion of microtubule associated proteins results in wider and longer tubulin-sheets than those polymerized in the presence of microtubule associated proteins. However by increasing zinc concentration wider but shorter tubulin-sheets were found. These results suggest that microtubule associated proteins and zinc could promote nucleation of tubulin-sheets, but zinc also promotes lateral tubulin-tubulin interaction. This interpretation was confirmed when microtubule protein was assembled at a low zinc:tubulin ratio. In such conditions composite structures of microtubules and zinc tubulin-sheets are formed. These composite structures are consequence of a lateral attachment of a zinc tubulin-sheet on a microtubule protofilament.

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Binding of Microtubule Proteins to DNA: Specificity of the Interaction

Cited by 46 publications

References 36 publications

Nuclear Tau and Its Potential Role in Alzheimer’s Disease

Nuclear Tau and Its Potential Role in Alzheimer’s Disease

Perinuclear Lamin A and Nucleoplasmic Lamin B2 Characterize Two Types of Hippocampal Neurons through Alzheimer’s Disease Progression

Factors implicated in determining the structure of zinc tubulin‐sheets: Lateral tubulin–tubulin interaction is promoted by the presence of zinc

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