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The Role of α-Synuclein and LRRK2 in Tau Phosphorylation.

Kawakami F, Ichikawa T - Parkinsons Dis (2015)

Bottom Line: There is now a considerable body of experimental evidence that Parkinson's disease arises through physiological interaction of causative molecules, leading to tau pathology.In this review, we discuss the physiological role of α-synuclein and LRRK2 in the abnormal phosphorylation of tau.In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to ameliorate neurodegenerative diseases associated with tau pathology, we also discuss therapeutic strategies for PD focusing on inhibition of α-synuclein- and LRRK2-associated tau phosphorylation by HSPs.

View Article: PubMed Central - PubMed

Affiliation: Department of Regulation Biochemistry, Graduate School of Medical Sciences, Kitasato University, Sagamihara 2520373, Japan.

ABSTRACT
There is now a considerable body of experimental evidence that Parkinson's disease arises through physiological interaction of causative molecules, leading to tau pathology. In this review, we discuss the physiological role of α-synuclein and LRRK2 in the abnormal phosphorylation of tau. In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to ameliorate neurodegenerative diseases associated with tau pathology, we also discuss therapeutic strategies for PD focusing on inhibition of α-synuclein- and LRRK2-associated tau phosphorylation by HSPs.

No MeSH data available.


Related in: MedlinePlus

LRRK2-mediated phosphorylation of tau.
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Related In: Results  -  Collection


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fig2: LRRK2-mediated phosphorylation of tau.

Mentions: We conclude that LRRK2 contributes to tau pathology through abnormal tau phosphorylation resulting from both direct and indirect mechanisms (Figure 2). In future studies, it will be necessary to identify the specific partners interacting with LRRK2 variants and the individual downstream pathways in order to understand the molecular mechanisms of abnormal tau phosphorylation associated with LRRK2. If a specific blocker of LRRK2 binding to interacting molecules could be identified, it might show promise as a drug for treatment of neurodegeneration associated with abnormal tau phosphorylation in PD.


The Role of α-Synuclein and LRRK2 in Tau Phosphorylation.

Kawakami F, Ichikawa T - Parkinsons Dis (2015)

LRRK2-mediated phosphorylation of tau.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4419261&req=5

fig2: LRRK2-mediated phosphorylation of tau.
Mentions: We conclude that LRRK2 contributes to tau pathology through abnormal tau phosphorylation resulting from both direct and indirect mechanisms (Figure 2). In future studies, it will be necessary to identify the specific partners interacting with LRRK2 variants and the individual downstream pathways in order to understand the molecular mechanisms of abnormal tau phosphorylation associated with LRRK2. If a specific blocker of LRRK2 binding to interacting molecules could be identified, it might show promise as a drug for treatment of neurodegeneration associated with abnormal tau phosphorylation in PD.

Bottom Line: There is now a considerable body of experimental evidence that Parkinson's disease arises through physiological interaction of causative molecules, leading to tau pathology.In this review, we discuss the physiological role of α-synuclein and LRRK2 in the abnormal phosphorylation of tau.In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to ameliorate neurodegenerative diseases associated with tau pathology, we also discuss therapeutic strategies for PD focusing on inhibition of α-synuclein- and LRRK2-associated tau phosphorylation by HSPs.

View Article: PubMed Central - PubMed

Affiliation: Department of Regulation Biochemistry, Graduate School of Medical Sciences, Kitasato University, Sagamihara 2520373, Japan.

ABSTRACT
There is now a considerable body of experimental evidence that Parkinson's disease arises through physiological interaction of causative molecules, leading to tau pathology. In this review, we discuss the physiological role of α-synuclein and LRRK2 in the abnormal phosphorylation of tau. In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to ameliorate neurodegenerative diseases associated with tau pathology, we also discuss therapeutic strategies for PD focusing on inhibition of α-synuclein- and LRRK2-associated tau phosphorylation by HSPs.

No MeSH data available.


Related in: MedlinePlus