Transient storage of a nuclear matrix protein along intermediate-type filaments during mitosis: a novel function of...

We recently identified a nuclear matrix protein, named NMP125 for its molecular weight (M(r) 125 kDa). On the basis of immunofluorescence analysis with monoclonal anti-NMP125 antibodies of differentially extracted cells in situ, including detergents, DNase I, RNase A, and high/low ionic strength conditions, it is concluded that NMP125 is a component of a chromatin- and histone-depleted nuclear substructure, operationally defined as nuclear matrix in interphase cells. The protein revealed evolutionary conservation in man, rat, chicken, and Xenopus, at least at the level of immunological crossreactivity. The subcellular distribution of NMP125 is cell-cycle-dependent; in interphase cells NMP125 is confined to a nuclear substructure with a granular aspect, whereas after nuclear envelope breakdown, it is freed into the cytoplasm. However, most of the protein remains attached to a cytoskeletal ligand that we have identified as the intermediate-type filament vimentin. In late mitotic stages the protein forms punctuate aggregates of relatively large size, which get passively closer to the newly formed telophase nuclei together with the reorganized vimentin around the nuclei in late telophase. From the morphological point of view, although static in nature, a dynamic cell-cycle-dependent distribution of NMP125 is found, revealing dissociation and spreading throughout the cytoplasm in metaphase, binding to vimentin filaments, cytoplasmic aggregation, and transport to nuclei in telophase. The transient affinity of the nuclear protein NMP125 to vimentin filaments during mitosis together with a passive cytoplasmic dislocation of the vimentin/NMP125 conjugate toward the telophase nuclei could represent a novel and dynamic function of cytoplasmic intermediate filaments, implicating a transient repository and passive shift of nuclear proteins during mitosis.