自噬是真核细胞中依赖溶酶体的降解途径。WIPI2在自噬前体膜长大延伸形成自噬体的过程中发挥关键作用，PI3P与WIPI2的结合为自噬前体膜招募WIPI2所必需。然而，WIPI2与PI3P的结合是否受到自噬信号的调控尚不明确。我们的前期研究发现，WIPI2不仅能结合VPS34复合物的催化产物PI3P，也能结合VPS34复合物本身。我们还发现，在诱导自噬的条件下，WIPI2与VPS34复合物之间的相互作用显著减弱。营养丰富条件下，内质网定位的VPS34复合物活性较低，自噬性PI3P合成很少。我们推测VPS34复合物结合WIPI2可能是为了防止WIPI2被招募至内吞体等处的PI3P上；营养缺乏条件下，WIPI2从激活的VPS34复合物处解离并特异性结合到自噬相关PI3P上发挥功能。本项研究，我们将深入探讨自噬信号调控自噬前体招募WIPI2的机制和功能，期待阐明WIPI2在自噬体形成中的作用机理。

Autophagy is a lysosome-dependent intracellular degradation pathway in eukaryotic cells. A key event for phagophore growth and expansion is the recruitment of WIPI2 by PI3P, synthesized by ER-localized VPS34 complex. WIPI2 then facilitates LC3 lipidation and the subsequent growth of the phagophore by recruiting Atg12-Atg5-Atg16L1 complex. However, whether the recruitment of WIPI2 to the phagophore is regulated by autophagy signaling remains unknown. In our preliminary work, we have found that WIPI2 not only binds PI3P but also interacts with its producers VPS34 complex 1 (containing Atg14) and VPS34 complex 2 (containing UVRAG). Intriguingly, the interaction between WIPI2 and VPS34 complex 1, but not complex 2, is dramatically suppressed during nutrient deprivation or Torin1 (mTOR inhibitor) treatment-induced autophagy. Under nutrient rich conditions, the synthesis of autophagic PI3P is inhibited, caused by the inactivation of VPS34 complex 1. The interaction between WIPI2 and VPS34 complex 1 may prevent the recruitment of WIPI2 to other PI3P-enriched cellular compartments such as endosomes. Under nutrient starvation, disassociation of WIPI2 from VPS34 complex 1 can facilitate WIPI2 to specifically target to autophagic PI3P. In this study, we will further investigate how autophagy signaling regulates the recruitment of WIPI2 to the phagophore. We aim to elucidate the underlying regulation mechanisms and function of WIPI2 in autophagosome formation.