Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 41, Pages 35863-35873Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.253450
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Funding
- Canadian Institutes of Health Research [MOP 84501, FRN 93603, MOP 84527]
- Alzheimer Association
- Parkinson Society of Canada
- Medical Research Council [MC_G1000734] Funding Source: researchfish
- MRC [MC_G1000734] Funding Source: UKRI
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Background: The majority of alpha-synuclein is phosphorylated at serine 129 in Lewy bodies. Results: The membrane association of PD-linked mutant alpha-synuclein, but not wild-type alpha-synuclein, was increased by serine 129 phosphorylation. Conclusion: Pathological serine 129 phosphorylation regulates membrane accumulation of mutant alpha-synuclein. Significance: The relationship of serine 129 phosphorylation to pathogenic aggregation of normal and mutant alpha-synuclein may be governed by distinct effects on phosphoprotein membrane accumulation.
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