vps-34 Antibody

VPS-34, the catalytic subunit of the PI3K complex, facilitates the formation of phosphatidylinositol 3-phosphate. In conjunction with bec-1, it mediates the production of phosphatidylinositol 3-phosphate on intracellular vesicles, thereby regulating membrane trafficking. This process is involved in the retrograde transport of mig-14 from endosomes to the Golgi apparatus. VPS-34 also plays a critical role in the clearance of apoptotic cell corpses via phagosomes. The maturation of phagosomes requires two distinct and non-overlapping pulses of phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface. This process mediates the recruitment of sorting nexins snx-1 and lst-4, along with small GTPases rab-5, rab-2, and rab-7, downstream of dynamin dyn-1. The initial pulse is initiated by piki-1, followed by sustained production by vps-34, which also generates the second pulse. VPS-34 is essential for embryonic development. Collaborating with bec-1, VPS-34 participates in the L3/L4 larval molting stage, likely by regulating cuticle shedding. Furthermore, VPS-34 regulates the expansion of the nuclear outer membrane, participates in the secretion and localization of lrp-1 at the apical surface of the hyp7 syncytium, and may regulate endocytosis in hypodermal cells. It is also implicated in the formation of gut granules, lysosome-related organelles, and potentially plays a role in germ stem cell proliferation during larval development.