The P6 protein of cauliflower mosaic virus (CaMV) is a multifunctional protein that forms the electron dense, amorphous inclusion bodies that accumulate in the cytoplasm and has been shown to physically interact with all other CaMV proteins, including the CaMV movement protein (P1). In this study, we have investigated the subcellular localization of the P6 and P1 proteins in transient expression assays in Nicotiana benthamiana, as well as the influence of P6 on the expression and subcellular localization of P1. A version of P6 tagged with RFP was shown to envelop the endoplasmic reticulum (ER), whereas P1 tagged with RFP was shown to induce the fragmentation of the ER. Co-expression of P6 with P1 led to an enhancement of the spatial and temporal expression of P1, with a shift from expression through the plasma membrane and interior of the cell to punctate spots associated with the cell wall.