Journal ArticleDOI
Tau as a nucleolar protein in human nonneural cells in vitro and in vivo.
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TLDR
The Tau-1 monoclonal antibody was localized to the nucleolus of interphase cells and the nucleolar organizing regions (NORs) of acrocentric chromosomes in cultured human cells, contributing to a growing body of evidence defining tau as a multifunctional protein that may be involved in ribosomal biogenesis and/or rRNA transcription in the nucleus of all cells as well as microtubule-stabilizing functions in the neuronal cytoplasm.Abstract:
The Tau-1 monoclonal antibody was localized to the nucleolus of interphase cells and the nucleolar organizing regions (NORs) of acrocentric chromosomes in cultured human cells. Putative nucleolar and NOR tau was found in HeLa cells and lymphoblasts as well as in nontransformed fibroblasts and lymphocytes. To confirm the presence of tau in the nuclei of these nonneural cells, immunoblotting analysis was performed on isolated nuclei from lymphoblasts. Several tau bands were noted on the blot of the nuclear extract suggesting the presence of multiple tau isoforms. Tau-1 immunostaining demonstrated variable staining intensities between individual acrocentric chromosomes in all cells tested. In cultured peripheral lymphocytes, these staining patterns were the same from one chromosome spread to the next within an individual. This consistency of Tau-1 staining and its variability among NORs was reminiscent of staining patterns obtained using the silver-NOR procedure. Comparisons of Tau-1 immunostaining with silver staining of chromosome spreads from human lymphocytes demonstrated that Tau-1 did not immunostain all of the NORs that were silver stained. The intensity of Tau-1 fluorescence in nucleoli was further shown to be increased in phytohemagglutinin-stimulated lymphocytes, indicating an upregulation of nuclear tau when cells reentered the cell cycle. These results contribute to a growing body of evidence defining tau as a multifunctional protein that may be involved in ribosomal biogenesis and/or rRNA transcription in the nucleus of all cells as well as microtubule-stabilizing functions in the neuronal cytoplasm.read more
Citations
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Journal ArticleDOI
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
TL;DR: Tau proteins are the major constituents of intraneuronal and glial fibrillar lesions described in Alzheimer's disease and numerous neurodegenerative disorders referred as 'tauopathies' as discussed by the authors.
Journal ArticleDOI
RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
TL;DR: It is reported that PHF assembly is strongly enhanced by RNA, dependent on the formation of intermolecular disulfide bridges involving Cys322 in the third repeat of tau and includes the dimerization of t Tau as an early intermediate.
Journal ArticleDOI
Tau interacts with src-family non-receptor tyrosine kinases
TL;DR: The data suggest that tau is involved in signal transduction pathways, and an interaction between tau and fyn may serve as a mechanism by which extracellular signals influence the spatial distribution of microtubules.
Journal ArticleDOI
Tau and tauopathies
TL;DR: According to currently emerging cell biological concepts, tau might play a role in the regulation of neuronal plasticity in a wide array of neuronal networks and in addition, it might be involved in regulating genome stability.
Journal ArticleDOI
Nuclear Tau, a Key Player in Neuronal DNA Protection
Audrey Sultan,Fabrice Nesslany,Marie Violet,Séverine Bégard,Anne Loyens,Smail Talahari,Zeyni Mansuroglu,Daniel Marzin,Nicolas Sergeant,Sandrine Humez,Morvane Colin,Eliette Bonnefoy,Luc Buée,Marie-Christine Galas +13 more
TL;DR: It is demonstrated that acute oxidative stress and mild heat stress induce the accumulation of dephosphorylated Tau in neuronal nuclei and a novel role for nuclear Tau as a key player in early stress response is highlighted.
References
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Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
Inge Grundke-Iqbal,Khalid Iqbal,Yunn-Chyn Tung,Maureen Quinlan,Henryk M. Wisniewski,Lester I. Binder +5 more
TL;DR: It is suggested that tau in Alzheimer brain is an abnormally phosphorylated protein component of PHF, the two major locations of paired-helical filaments in Alzheimer disease brain.
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Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
TL;DR: Antisera raised against synthetic peptides corresponding to these different human tau isoforms demonstrate that multiple tau protein isoforms are incorporated into the neurofibrillary tangles of Alzheimer's disease.