α-Synuclein plasma membrane localization correlates with cellular phosphatidylinositol polyphosphate levels.

Cédric Eichmann, Alessandro Dema, Davide Mercadante, Philipp Selenko

Research output: Contribution to journalArticlepeer-review

Abstract

The Parkinson’s disease protein α-synuclein (αSyn) promotes membrane fusion and fission by interacting with various negatively charged phospholipids. Despite postulated roles in endocytosis and exocytosis, plasma membrane (PM) interactions of αSyn are poorly understood. Here, we show that phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3), two highly acidic components of inner PM leaflets, mediate plasma membrane localization of endogenous pools of αSyn in A2780, HeLa, SK-MEL-2 and differentiated and undifferentiated neuronal SH-SY5Y cells. We demonstrate that αSyn binds to reconstituted PIP2-membranes in a helical conformation in vitro and that PIP2 synthesizing kinases and hydrolyzing phosphatases reversibly redistribute αSyn in cells. We further delineate that αSyn-PM targeting follows phosphoinositide-3 kinase (PI3K)-dependent changes of cellular PIP2 and PIP3 levels, which collectively suggests that phosphatidylinositol polyphosphates contribute to αSyn’s cellular function(s) at the plasma membrane.
Original languageEnglish
Article numbere61951
Number of pages21
JournaleLife
Volume10
DOIs
StatePublished Online - 15 Feb 2021

Fingerprint

Dive into the research topics of 'α-Synuclein plasma membrane localization correlates with cellular phosphatidylinositol polyphosphate levels.'. Together they form a unique fingerprint.

Cite this