. alpha-Synuclein interacts with phospholipase D isozymes and inhibits pervanadate-induced phospholipase D activation in human embryonic kidney-293 cells. J Biol Chem. 2002 Apr 5;277(14):12334-42. PubMed.

Recommends

Please login to recommend the paper.

Comments

Make a Comment

To make a comment you must login or register.

Comments on this content

  1. Although understanding factors regulating aggregation of a-synuclein is perhaps the most relevant issue to neurodegeneration, understanding the normal function and regulation of a-synuclein remains fundamentally important to the field. Insights into synuclein biology help us to understand its role in the brain, and might also shed light on novel factors that might be relevant to synucleinopathies. This paper expands upon prior work showing that synuclein inhibits phospholipase D by identifying the regions of synuclein important for this interaction. Interestingly, the site of interaction of a-synuclein with phospholipase D is close to a region of a-synuclein that is critical for its aggregation, although phospholipase D does not appear to directly modulate synuclein aggregation.