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A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies. / Ubhi, Kiren K.; Shaibah, Hassan; Newman, Tracey A. et al.
In: Invertebrate neuroscience, Vol. 7, No. 3, 09.2007, p. 165-71.

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Ubhi, KK, Shaibah, H, Newman, TA, Shepherd, D & Mudher, A 2007, 'A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies', Invertebrate neuroscience, vol. 7, no. 3, pp. 165-71. https://doi.org/10.1007/s10158-007-0052-4

APA

Ubhi, K. K., Shaibah, H., Newman, T. A., Shepherd, D., & Mudher, A. (2007). A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies. Invertebrate neuroscience, 7(3), 165-71. https://doi.org/10.1007/s10158-007-0052-4

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MLA

VancouverVancouver

Ubhi KK, Shaibah H, Newman TA, Shepherd D, Mudher A. A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies. Invertebrate neuroscience. 2007 Sept;7(3):165-71. doi: 10.1007/s10158-007-0052-4

Author

Ubhi, Kiren K. ; Shaibah, Hassan ; Newman, Tracey A. et al. / A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies. In: Invertebrate neuroscience. 2007 ; Vol. 7, No. 3. pp. 165-71.

RIS

TY - JOUR

T1 - A comparison of the neuronal dysfunction caused by Drosophila tau and human tau in a Drosophila model of tauopathies

AU - Ubhi, Kiren K.

AU - Shaibah, Hassan

AU - Newman, Tracey A.

AU - Shepherd, David

AU - Mudher, Amritpal

PY - 2007/9

Y1 - 2007/9

N2 - Hyperphosphorylation and aggregation of tau into tangles is a feature of disorders such as Alzheimer's disease and other Tauopathies. To model these disorders in Drosophila melanogaster, human tau has been over-expressed and a variety of phenotypes have been observed including neurotoxicity, disrupted neuronal and synaptic function and locomotor impairments. Neuronal dysfunction has been seen prior to neuronal death and in the absence of tangle formation. The Drosophila tau protein shares a large degree of homology with human tau but differs in the crucial microtubule binding domains. Although like human tau Drosophila tau can induce neurotoxicity, little is known about its ability to disrupt neuronal function. In this study we demonstrate that like human tau, over-expression of Drosophila tau results in disrupted axonal transport, altered neuromuscular junction morphology and locomotor impairments. This indicates that like human tau, over-expression of Drosophila tau compromises neuronal function despite significant differences in microtubule binding regions.

AB - Hyperphosphorylation and aggregation of tau into tangles is a feature of disorders such as Alzheimer's disease and other Tauopathies. To model these disorders in Drosophila melanogaster, human tau has been over-expressed and a variety of phenotypes have been observed including neurotoxicity, disrupted neuronal and synaptic function and locomotor impairments. Neuronal dysfunction has been seen prior to neuronal death and in the absence of tangle formation. The Drosophila tau protein shares a large degree of homology with human tau but differs in the crucial microtubule binding domains. Although like human tau Drosophila tau can induce neurotoxicity, little is known about its ability to disrupt neuronal function. In this study we demonstrate that like human tau, over-expression of Drosophila tau results in disrupted axonal transport, altered neuromuscular junction morphology and locomotor impairments. This indicates that like human tau, over-expression of Drosophila tau compromises neuronal function despite significant differences in microtubule binding regions.

KW - Animals

KW - Animals, Genetically Modified

KW - Axonal Transport/physiology

KW - Disease Models, Animal

KW - Drosophila/metabolism

KW - Drosophila Proteins/metabolism

KW - Humans

KW - Immunohistochemistry

KW - Larva

KW - Movement/physiology

KW - Neuromuscular Junction/pathology

KW - Neurons/metabolism

KW - Tauopathies/metabolism

KW - tau Proteins/metabolism

U2 - 10.1007/s10158-007-0052-4

DO - 10.1007/s10158-007-0052-4

M3 - Article

C2 - 17636367

VL - 7

SP - 165

EP - 171

JO - Invertebrate neuroscience

JF - Invertebrate neuroscience

SN - 1354-2516

IS - 3

ER -