Cells utilise signalling networks to rapidly respond to environmental cues and initiate appropriate biological responses. These responses arise from a dynamic balance between feedforward signals and feedback regulation, whereby information is relayed to enhance or suppress signal flow as needed. Activation of the protein kinase Akt must be tightly controlled, as it is a key node in a range of signal transduction cascades which regulate fundamental processes such as cell proliferation and metabolism. Disruption of this control can give rise to a plethora of diseases - for example, Akt is often hyperactivated in cancer. It is of upmost importance to understand how Akt activity is regulated in the cell, to inform the design of appropriate therapeutic interventions which can ameliorate abnormal Akt activation in disease. Using live cell total internal reflection fluorescence (TIRF) microscopy, we have discovered a potent feedback mechanism which reduces signal flow across the Akt signalling axis. Our data suggest that following Akt activation in response to growth factors, Akt reduces phosphoinositide 3-kinase (PI3K) activity and subsequently lowers the amount of phosphatidylinositol (3,4,5)-trisphosphate (PIP3) present at the cell surface. This limits Akt recruitment to the plasma membrane thereby negatively regulating its kinase activity, and consequently the many physiological processes Akt orchestrates. Thus, our findings pinpoint a novel feedback loop which prevents hyperactivation of Akt. This will guide future endeavours to fine-tune Akt activity in disease states which are associated with aberrant Akt signalling.