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Clathrin mediated endocytosis (CME) is an ubiquitous cellular pathway thatregulates central aspects of cell physiology such as nutrient uptake,modulation of signal transduction, synaptic transmission and membraneturn-over. Endocytic vesicle formation depends on the timed production ofspecific phosphoinositides and their interactions with various endocyticproteins. Recently, it has been found thatphosphatidylinositol-3,4-bisphosphate (PI(3,4)P2) produced by the class IIphosphatidylinositol 3-kinase C2alpha plays a key role in the recruitment ofthe PX-BAR domain protein SNX9, which is proposed to play a role in theconstriction of the endocytic vesicle neck [Posor et al, Nature 499, p233(2013)]. Interestingly, SNX9 and its close paralog SNX18 are not fully specificto PI(3,4)P2 but can also bind other phospholipids, in particular to PI(4,5)P2,an abundant plasma membrane lipid required for the recruitment of manyendocytic proteins. In order to understand the dynamical interplay betweenphospholipids and endocytic proteins, we developed a computational model of thetemporal changes in the population of the phosphoinositide-associated endocyticproteins and their spatial distribution at a clathrin-coated pit (CCP). Themodel resolves single molecules in time and space, and incorporates the complexinterplay of proteins and lipids, as well as their movement within the CCP. Wefind that the comparably small differences in lipid binding affinities ofendocytic proteins are amplified by competition among them, allowing for theselective enrichment of SNX9 at late stage CCPs as a result of timed PI(3,4)P2production.

Spatiotemporal model of a key step in endocytosis: SNX9 recruitment via phosphoinositides