Rhabdoviruses infect a wide range of hosts that includes humans, terrestrial animals/vertebrates, fish, arthropods, and plants. The genomes of the plant-adapted viruses are organized generally into into seven open reading frames with the gene order 3’-N-X-P-Y-M-G-L-5’, which encodes the nucleocapsid, phospho, movement, matrix, glyco, and RNA-dependent RNA polymerase proteins, respectively, except for X, which is of unknown function. In addition to its structural role in virion formation, the M protein of Potato yellow dwarf virus (PYDV) is capable of inducing the intranuclear accumulation of the inner nuclear membranes (INM) in transfected cells. The M protein also interacts with the nuclear import and export receptors Importin-alpha and Exportin 1, suggesting a role for M in transport of condensed nucleocapsids from the nucleus. Interestingly, the ability to remodel the INM is conferred by the P, but not M, protein of coffee ringspot dichorhavirus, demonstrating that functional domains within rhabdoviral proteins are portable. This variation likely contributes to the finding protein interaction and localization maps (PILMs) for each virus are unique. Efforts to map the plant nucleome, the nuclear-associated portion of the proteome, show that nucleorhabdoviruses induce dramatic changes in the localization patterns of nuclear proteins, some of which are recruited to sites of viral replication and assembly.