Cell polarity or cell asymmetry is crucial for the normal biological function of all metazoan cells. Loss of cell polarity disrupts cellular organisation that represents one of the hallmark of cancer progression. A core polarity module named SCRIB is found to be part of the establishment and maintenance of cell polarity. Scribble, a member of the SCRIB module is found to be deregulated in many cancers such as breast cancer, cervical cancer and prostate cancer. Scribble is a member of the LAP family that consists of 16 Leucine Rich Repeats and 4 PDZ domains. These domains allow Scribble to interact with different molecules that are involved in many signalling pathways. We hypothesised that Scribble acts as a scaffold protein to mediate these interactions. This project aims to decipher Scribble’s mechanism of action by investigating its interactions with betaPIX (PAK-interacting exchange factor beta). Scribble’s interaction with betaPIX has been showed to be important for exocytosis, neuronal transmission and directed migration. In this study we expressed, purified and characterised each individual Scribble domain and evaluated their interactions with betaPIX using multiple biochemical methods. We then determined the solution structure of a fragment of Scribble comprising all four PDZ domains using small angle X-ray scattering in conjunction with high-resolution NMR and crystal structures. Our study suggests the nature of Scribble and betaPIX interaction may be dependent on their specific sub-cellular localisation as well as the quarternary structure of Scribble.