The peptidyl prolyl cis/trans isomerase Pin1/Ess1 inhibits phosphorylation and toxicity of tau in a yeast model for Alzheimer’s disease

Vos, Ann De; Bynens, Tine; Rosseels, Joëlle; Coun, Catherina; Ring, Julia; Madeo, Frank; Galas, Marie‐Christine; Winderickx, Joris; Franssens, Vanessa

doi:10.3934/molsci.2015.2.144

Cited by 8 publications

(13 citation statements)

References 46 publications

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“…Additionally, deficiencies of Ess1 were shown to slow yeast growth, increase inclusion formation of human tau, and led to tau toxicity which could be restored by the expression of Pin1. Contrary to results 45 discussed above, it is suggested that the accumulation of hyperphosphorylated and aggregationprone tau causes cytotoxicity in yeast 47 . This study specifically validates yeast as a powerful model to study the effect of human isomerase Pin1 and its biological interplay with tau regarding its phosphorylation and aggregation.…”

Section: Yeast Contribution To the Study Of Tau Biologycontrasting

confidence: 70%

Yeast contributions to Alzheimer’s Disease

McDonald¹,

Dhakal²,

Macreadie³

2020

J Human Clin Gen

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Alzheimer's Disease is a highly prevalent, age-related, neurodegenerative disease associated with the accumulation of toxic proteins, including amyloid beta and tau, that affect important cellular functions. Through the study of these proteins in yeast over the past 2 decades, the effects of amyloid beta oligomerization and aggregation, and tau hyperphosphorylation on basic cellular functions, such as ageing, oxidative stress, cell cycling and proteostasis have been observed. Strategies for the prevention of damage by these proteins can be explored, thanks to the exquisite array of technologies available for yeast studies. This review summarises existing knowledge of Alzheimer's Disease, the work over the past two decades on yeast models for Alzheimer's Disease and how these models contribute to the development of treatments and preventative strategies for Alzheimer's Disease.

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Section: Yeast Contribution To the Study Of Tau Biologycontrasting

confidence: 70%

Yeast contributions to Alzheimer’s Disease

McDonald¹,

Dhakal²,

Macreadie³

2020

J Human Clin Gen

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“…Pin1, a peptidyl prolyl cis / trans isomerase, can then subsequently activate Phosphatase 2a. De Vos and colleagues reported, in accordance with this finding, that a dysfunctional Ess1, Pin1’s yeast orthologue, increases Tau hyperphosphorylation [ 93 ].…”

Section: Humanized Yeast Models To Study Tau Biologymentioning

confidence: 58%

Recent Insights on Alzheimer’s Disease Originating from Yeast Models

Seynnaeve

Vecchio

Fruhmann

et al. 2018

IJMS

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In this review article, yeast model-based research advances regarding the role of Amyloid-β (Aβ), Tau and frameshift Ubiquitin UBB+1 in Alzheimer’s disease (AD) are discussed. Despite having limitations with regard to intercellular and cognitive AD aspects, these models have clearly shown their added value as complementary models for the study of the molecular aspects of these proteins, including their interplay with AD-related cellular processes such as mitochondrial dysfunction and altered proteostasis. Moreover, these yeast models have also shown their importance in translational research, e.g., in compound screenings and for AD diagnostics development. In addition to well-established Saccharomyces cerevisiae models, new upcoming Schizosaccharomyces pombe, Candida glabrata and Kluyveromyces lactis yeast models for Aβ and Tau are briefly described. Finally, traditional and more innovative research methodologies, e.g., for studying protein oligomerization/aggregation, are highlighted.

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“…On the other hand, oxidative stress could also induce a Pin1 mediated activation of protein phosphatase 2A (Galas et al, 2006). This is supported by the finding that disruption of Ess1, the yeast orthologue of Pin1, induced Tau hyperphosphorylation (De Vos et al, 2015).…”

Section: Aβ Deposits As a Hallmark Of Alzheimer's Diseasementioning

confidence: 90%