Tau Phosphorylation, Aggregation, and Cell Toxicity
نویسندگان
چکیده
منابع مشابه
Tau Phosphorylation, Aggregation, and Cell Toxicity
Protein aggregation takes place in many neurodegenerative disorders. However, there is a controversy about the possible toxicity of these protein aggregates. In this review, this controversy is discussed, focussing on the tau aggregation that takes place in those disorders known as tauopathies.
متن کاملFrom tau phosphorylation to tau aggregation: what about neuronal death?
Tau pathology is characterized by intracellular aggregates of abnormally and hyperphosphorylated tau proteins. It is encountered in many neurodegenerative disorders, but also in aging. These neurodegenerative disorders are referred to as tauopathies. Comparative biochemistry of the tau aggregates shows that they differ in both tau isoform phosphorylation and content, which enables a molecular c...
متن کاملPhosphorylation differentiates tau-dependent neuronal toxicity and dysfunction.
The heterogeneous pathology of tauopathies and the differential susceptibility of different neuronal types to WT (wild-type) and mutant tau suggest that phosphorylation at particular sites rather than hyperphosphorylation mediates toxicity or dysfunction in a cell-type-specific manner. Pan-neuronal accumulation of tau in the Drosophila CNS (central nervous system) specifically affected the MBs ...
متن کاملSite-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation.
The microtubule-associated protein tau is hyperphosphorylated and forms neurofibrillary tangles in Alzheimer disease. Additionally caspase-cleaved tau is present in Alzheimer disease brains co-localized with fibrillar tau pathologies. To further understand the role of site-specific phosphorylation and caspase cleavage of tau in regulating its function, constructs of full-length tau (T4) or tau ...
متن کاملIdentification of the Tau phosphorylation pattern that drives its aggregation.
Determining the functional relationship between Tau phosphorylation and aggregation has proven a challenge owing to the multiple potential phosphorylation sites and their clustering in the Tau sequence. We use here in vitro kinase assays combined with NMR spectroscopy as an analytical tool to generate well-characterized phosphorylated Tau samples and show that the combined phosphorylation at th...
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ژورنال
عنوان ژورنال: Journal of Biomedicine and Biotechnology
سال: 2006
ISSN: 1110-7243,1110-7251
DOI: 10.1155/jbb/2006/74539