RGD Reference Report - alpha-Synuclein interacts with phospholipase D isozymes and inhibits pervanadate-induced phospholipase D activation in human embryonic kidney-293 cells. - Rat Genome Database

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alpha-Synuclein interacts with phospholipase D isozymes and inhibits pervanadate-induced phospholipase D activation in human embryonic kidney-293 cells.

Authors: Ahn, BH  Rhim, H  Kim, SY  Sung, YM  Lee, MY  Choi, JY  Wolozin, B  Chang, JS  Lee, YH  Kwon, TK  Chung, KC  Yoon, SH  Hahn, SJ  Kim, MS  Jo, YH  Min, DS 
Citation: Ahn BH, etal., J Biol Chem. 2002 Apr 5;277(14):12334-42. Epub 2002 Jan 30.
RGD ID: 2291795
Pubmed: PMID:11821392   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M110414200   (Journal Full-text)

alpha-Synuclein has been implicated in the pathogenesis of many neurodegenerative diseases, including Parkinson's disease and Alzheimer's disease. Although the function of alpha-synuclein remains largely unknown, recent studies have demonstrated that this protein can interact with phospholipids. To address the role of alpha-synuclein in neurodegenerative disease, we have investigated whether it binds phospholipase D (PLD) and affects PLD activity in human embryonic kidney (HEK)-293 cells overexpressing wild type alpha-synuclein or the mutant forms of alpha-synuclein (A53T, A30P) associated with Parkinson's disease. Tyrosine phosphorylation of alpha-synuclein appears to play a modulatory role in the inhibition of PLD, because mutation of Tyr(125) to Phe slightly increases inhibitory effect of alpha-synuclein on PLD activity. Treatment with pervanadate or phorbol myristate acetate inhibits PLD more in HEK 293 cells overexpressing alpha-synuclein than in control cells. Binding of alpha-synuclein to PLD requires phox and pleckstrin homology domain of PLD and the amphipathic repeat region and non-Abeta component of alpha-synuclein. Although biologically important, co-transfection studies indicate that the interaction of alpha-synuclein with PLD does not influence the tendency of alpha-synuclein to form pathological inclusions. These results suggest that the association of alpha-synuclein with PLD, and modulation of PLD activity, is biologically important, but PLD does not appear to play an essential role in the pathophysiology of alpha-synuclein.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
phospholipase binding  IPIPLD1 (Homo sapiens)2291795 RGD 
protein domain specific binding  IPIPLD1 (Homo sapiens)2291795 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Snca  (synuclein alpha)


Additional Information