TAp73α induces tau phosphorylation in HEK293a cells via a transcription-dependent mechanism

Claudie Hooper; Richard Killick; Mahvash Tavassoli; Gerry Melino; Simon Lovestone

doi:10.1016/j.neulet.2006.02.082

TAp73α induces tau phosphorylation in HEK293a cells via a transcription-dependent mechanism

Claudie Hooper, Richard Killick, Mahvash Tavassoli, Gerry Melino, Simon Lovestone

Istituto Dermopatico dell'Immacolata , IDI

Research output: Contribution to journal › Article › peer-review

Abstract

p73 and tau both play roles in neurodevelopment and neurodegeneration. In this pilot study we show by Western blotting that TAp73α induces phosphorylation of human 2N4R tau at threonine-205 and at the PHF-1 epitope (serine366/serine404) in HEK293a cells. Neither the dominant negative isoform, ΔNp73, nor a transcriptionally inactive mutant TAp73α_R292H altered tau phosphorylation indicating that tau phosphorylation is dependent on the transcriptional activity of TAp73α. Consistent with this, confocal microscopy revealed that tau and TAp73α were spatially separated within the cell; tau being located in the cytoskeletal compartment whilst TAp73α was found in the nucleus. These findings have ramifications for microtubule dynamics associated with axonal growth during development and for neuronal death associated with Alzheimer's disease and other tauopathies.

Original language	English
Pages (from-to)	30-34
Number of pages	5
Journal	Neuroscience Letters
Volume	401
Issue number	1-2
DOIs	https://doi.org/10.1016/j.neulet.2006.02.082
Publication status	Published - Jun 19 2006

Keywords

Alzheimer's disease
Microtubules
Neurodevelopment
p53
p73
Tau

ASJC Scopus subject areas

Neuroscience(all)

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10.1016/j.neulet.2006.02.082

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title = "TAp73α induces tau phosphorylation in HEK293a cells via a transcription-dependent mechanism",

abstract = "p73 and tau both play roles in neurodevelopment and neurodegeneration. In this pilot study we show by Western blotting that TAp73α induces phosphorylation of human 2N4R tau at threonine-205 and at the PHF-1 epitope (serine366/serine404) in HEK293a cells. Neither the dominant negative isoform, ΔNp73, nor a transcriptionally inactive mutant TAp73αR292H altered tau phosphorylation indicating that tau phosphorylation is dependent on the transcriptional activity of TAp73α. Consistent with this, confocal microscopy revealed that tau and TAp73α were spatially separated within the cell; tau being located in the cytoskeletal compartment whilst TAp73α was found in the nucleus. These findings have ramifications for microtubule dynamics associated with axonal growth during development and for neuronal death associated with Alzheimer's disease and other tauopathies.",

keywords = "Alzheimer's disease, Microtubules, Neurodevelopment, p53, p73, Tau",

author = "Claudie Hooper and Richard Killick and Mahvash Tavassoli and Gerry Melino and Simon Lovestone",

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doi = "10.1016/j.neulet.2006.02.082",

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journal = "Neuroscience Letters",

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T1 - TAp73α induces tau phosphorylation in HEK293a cells via a transcription-dependent mechanism

AU - Hooper, Claudie

AU - Killick, Richard

AU - Tavassoli, Mahvash

AU - Melino, Gerry

AU - Lovestone, Simon

PY - 2006/6/19

Y1 - 2006/6/19

N2 - p73 and tau both play roles in neurodevelopment and neurodegeneration. In this pilot study we show by Western blotting that TAp73α induces phosphorylation of human 2N4R tau at threonine-205 and at the PHF-1 epitope (serine366/serine404) in HEK293a cells. Neither the dominant negative isoform, ΔNp73, nor a transcriptionally inactive mutant TAp73αR292H altered tau phosphorylation indicating that tau phosphorylation is dependent on the transcriptional activity of TAp73α. Consistent with this, confocal microscopy revealed that tau and TAp73α were spatially separated within the cell; tau being located in the cytoskeletal compartment whilst TAp73α was found in the nucleus. These findings have ramifications for microtubule dynamics associated with axonal growth during development and for neuronal death associated with Alzheimer's disease and other tauopathies.

AB - p73 and tau both play roles in neurodevelopment and neurodegeneration. In this pilot study we show by Western blotting that TAp73α induces phosphorylation of human 2N4R tau at threonine-205 and at the PHF-1 epitope (serine366/serine404) in HEK293a cells. Neither the dominant negative isoform, ΔNp73, nor a transcriptionally inactive mutant TAp73αR292H altered tau phosphorylation indicating that tau phosphorylation is dependent on the transcriptional activity of TAp73α. Consistent with this, confocal microscopy revealed that tau and TAp73α were spatially separated within the cell; tau being located in the cytoskeletal compartment whilst TAp73α was found in the nucleus. These findings have ramifications for microtubule dynamics associated with axonal growth during development and for neuronal death associated with Alzheimer's disease and other tauopathies.

KW - Alzheimer's disease

KW - Microtubules

KW - Neurodevelopment

KW - p53

KW - p73

KW - Tau

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TAp73α induces tau phosphorylation in HEK293a cells via a transcription-dependent mechanism

Abstract

Keywords

ASJC Scopus subject areas

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