Expression of RNUDC, a potential nuclear movement protein, in mammalian cells: localization to the Golgi apparatus

Prolactin and other cytokines regulate lymphocyte proliferation through the activation of a number of genes, one of which was identified as RnudC from a prolactin-dependent rat T cell line, Nb2. RnudC encodes a 45-kDa protein whose carboxy terminal 94 amino acids are similar to the carboxy terminus of the Aspergillus nidulans nuclear movement protein NUDC. In Nb2 T cells, RNUDC protein levels are induced two- to threefold by prolactin stimulation. This prolactin-inducible increase in RNUDC protein levels is due in part to an increase in RNUDC protein synthesis between 8 and 12 h, during the G1/S transition. Newly synthesized RNUDC protein is very stable, exhibiting a half-life of greater than 8 h. RNUDC has also been identified in many different cell types and species, ranging from fibroblasts to neuronal cells and from mouse to human, suggesting a highly conserved function. Immunocytochemical studies, using affinity-purified rabbit anti-rat RNUDC antibodies, have localized a significant fraction of the RNUDC protein to the region of the Golgi apparatus in interphase rat Nb2 T cells, monkey kidney fibroblast COS-1 cells, and human 2AG10 adenocarcinoma cells. Treatment of 2AG10 cells with the microtubule-depolymerizing drug nocodazole, which causes dispersion of the Golgi apparatus, led to a diffuse pattern of RNUDC staining. Removal of nocodazole, which allowed the reformation of the Golgi apparatus, led to the reconcentration of RNUDC staining to the Golgi region. Taken together, these studies suggest that a fraction of RNUDC is tightly associated with the Golgi apparatus in many different mammalian cell types.