MDCK cells form epithelial monolayer like structure when grown to the confluence on a glass substrate. We found that GRASP65 translocates to the plasma membrane from the Golgi apparatus. GRASP65 stimulate the ER to Golgi transport functioning as a target molecule for the ER derived transport vesicles coming into the Golgi apparatus. Therefore, it was suggested that GRASP65 plays a role in atypical secretary pathway that bypasses the Golgi apparatus during the epithelial monolayer formation. Morphological and biochemical analyses revealed the possibility that phosphorylated GRASP65 translocated from the Golgi apparatus to the plasma membrane. However, the cross-reaction of the antibody with beta-catenin hampered the confirmation of the phosphorylated GRASP65 to the plasma membrane. As the over expressed GRSAP65 localized to the plasma membrane, it is still probable that phosphorylated GRASP65 translocates to the plasma membrane. The cross-reaction with beta-catenin even suggested the existence of a common ligand to phosphorylated GRASP65 and beta-catenin implying the cross talk between GRASP65 and beta-catenin.