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J. Biol. Chem., Vol. 275, Issue 28, 21364-21371, July 14, 2000

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Interferon- Induces Nmi-IFP35 Heterodimeric Complex Formation That Is Affected by the Phosphorylation of IFP35^*

Xiangjun Zhou^§, Jian Liao^¶, Anke Meyerdierks, Li Feng, Louie Naumovski^**, Erik C. Böttger, and M. Bishr Omary

From the  Palo Alto Veterans Affairs Medical Center and Stanford University, Palo Alto, California 94304, the  Institut für Medizinische Mikrobiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany, and the ^** Department of Pediatrics, Stanford University, Stanford, California 94305

Nmi and IFP35 are interferon (IFN)-induced proteins. In cells treated with IFN-, Nmi enhances the association of transcription co-activator CBP/p300 with signal transducer and activator of transcription proteins, and IFP35 forms a high molecular weight cytosolic complex of unknown constituents. Here we show that Nmi and IFP35 co-immunoprecipitate with an anti-keratin 19 antibody, which is due to cross-reaction of the antibody with Nmi, and suggests an Nmi-IFP35 physical association. In support of this, Nmi and IFP35 co-immunoprecipitate using anti-Nmi and anti-IFP35 antibodies, manifest enhanced colocalization as determined by immunofluorescence staining of IFN-treated cells, and form heterodimers as determined by chemical cross-linking. Nmi and IFP35 are primarily cytosolic proteins, and their interaction is increased after IFN- treatment of cells as early as 1 h after exposure. Sucrose gradient sedimentation and size fractionation showed a shift of Nmi-IFP35 heterodimers toward a heavier fraction (100-200 kDa) in IFN--treated cells. This dynamic complex formation is reversed by pretreatment with okadaic acid. Two-dimensional gel analysis indicates that the IFN-induced complex formation correlates with IFP35 dephosphorylation. Our data demonstrate Nmi-IFP35 cytosolic localization and heterodimerization, and an IFN--regulated molecular event in which Nmi and IFP35 participate, reversibly and by a dephosphorylation dependent fashion, in a 100-200-kDa molecular complex formation.

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