Formation of these structures required the C-terminal BAR domain as well as the adjacent Phox homology (PX) domain of Sh3px1. In addition, we demonstrate that over-expression of Sh3px1 in S2 cells results in the formation of tubules as well as long protrusions. A similar phenotype has been reported upon depletion of Scar, the actin nucleation factor implicated in forming lamellipodia. We found that depletion of Sh3px1 from Drosophila Schneider 2 (S2) cells resulted in defective lamellipodia formation. In this report, we present our initial characterization of sh3px1. The Snx9 family is encoded by a single gene in Drosophila called sh3px1. In addition to endocytosis, recent studies have implicated the Snx9 family in diverse processes such as autophagy, macropinocytosis, phagocytosis and mitosis. BAR domains are known to sense and/or induce membrane curvature. In addition to the Sh3 domain, Snx9 also contains a C-terminal BAR domain. Snx9 contains an Sh3 domain at its N-terminus and has been shown to interact with Dynamin and actin nucleation factors via this domain. Most of the published literature to date has centered on the role of Snx9 in clathrin-mediated endocytosis (CME). The mammalian Sorting Nexin 9 (Snx9) family consists of three paralogs: Snx9, Snx18 and Snx33.
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