Mitosis-Specific Phosphorylation of Vimentin by Protein Kinase C Coupled with Reorganization of Intracellular Membranes

Using two types of anti-phosphopeptide antibodies which specifically recognize vimentin phosphorylated by protein kinase C (PKC) at two distinct PKC sites, we found that PKC acted as a mitotic vimentin kinase. Temporal change of vimentin phosphorylation by PKC differed from changes by cdc2 kinase. T...

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Bibliographic Details
Published in:The Journal of cell biology 1996-04, Vol.133 (1), p.141-149
Main Authors: Takai, Yasushi, Ogawara, Midori, Tomono, Yasuko, Moritoh, Chiharu, Imajoh-Ohmi, Shinobu, Tsutsumi, Osamu, Taketani, Yuji, Inagaki, Masaki
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies
Antibodies, Monoclonal
Antibody Specificity
Astrocytoma
Cattle
CDC2 Protein Kinase - metabolism
Cell Compartmentation
Cell cycle
Cell Division
Cell Line
Cells
Cellular biology
Cytosol
Enzyme Activation
Humans
Interphase
Intracellular membranes
Intracellular Membranes - metabolism
Membranes
Mitosis
Mitosis - physiology
Molecular Sequence Data
Phospholipids - physiology
Phosphopeptides - analysis
Phosphorylation
Protein Kinase C - metabolism
Proteins
Tetradecanoylphorbol Acetate - pharmacology
Tumor Cells, Cultured
Vimentin
Vimentin - metabolism
Western blotting
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Summary:Using two types of anti-phosphopeptide antibodies which specifically recognize vimentin phosphorylated by protein kinase C (PKC) at two distinct PKC sites, we found that PKC acted as a mitotic vimentin kinase. Temporal change of vimentin phosphorylation by PKC differed from changes by cdc2 kinase. The mitosis-specific vimentin phosphorylation by PKC was dramatically enhanced by treatment with a PKC activator, 12-O-tetradecanoylphorbol-13-acetate (TPA), while no phosphorylation of vimentin by PKC was observed in interphase cells treated with TPA. By contrast, the disruption of subcellular compartmentalization of interphase cells led to vimentin phosphorylation by PKC. Cytoplasmic and nuclear membranes are fragmented and dispersed in the cytoplasm and some bind to vimentin during mitosis. Thus, targeting of activated PKC, coupled with the reorganization of intracellular membranes which contain phospholipids essential for activation, leads to the mitosis-specific phosphorylation of vimentin. We propose that during mitosis, PKC may phosphorylate an additional subset of proteins not phosphorylated in interphase.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.133.1.141