期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 47, 期 -, 页码 827-838出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST20180466
关键词
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资金
- DFG Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB)
- Medical Research Council [MR/M00676X/1]
- Galician Government (Programa de axudas a etapa posdoutoral, XUGA, GAIN) [ED481B 2017/053]
- [SFB1286]
- MRC [MR/M00676X/1] Funding Source: UKRI
- Medical Research Council [MR/M00676X/1] Funding Source: researchfish
The identification of genetic forms of Parkinson's disease (PD) has tremendously expanded our understanding of the players and mechanisms involved. Mutations in the genes encoding for alpha-synuclein (aSyn), LRRK2, and tau have been associated with familial and sporadic forms of the disease. aSyn is the major component of Lewy bodies and Lewy neurites, which are pathognomonic protein inclusions in PD. Hyperphosphorylated tau protein accumulates in neurofibrillary tangles in the brains of Alzheimer's disease patients but is also seen in the brains of PD patients. LRRK2 is a complex multi-domain protein with kinase and GTPase enzymatic activity. Since aSyn and tau are phosphoproteins, we review the possible interplay between the three proteins. Understanding the interplay between LRRK2, aSyn and tau is extremely important, as this may enable the identification of novel targets and pathways for therapeutic intervention.
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