Association of the beta isoform of protein kinase C with vimentin filaments.
Association of the beta isoform of protein kinase C with vimentin filaments.
复制标题
蛋白激酶 C β 亚型与波形蛋白丝的关联。
DOI:
10.1002/cm.970220405
复制
发表时间:
1992
影响因子:
--
通讯作者:
Stryer,L
中科院分区:
文献类型:
--
作者:
Spudich,A;Meyer,T;Stryer,L
Protein kinase C (PKC) isoforms are key mediators in hormone, growth factor, and neurotransmitter triggered pathways of cell activation (Nishizuka: Science 233: 305-312, 1986; Nature 334: 661-665, 1988). Stimulation of kinase activity by diacylglycerol and calcium often leads to translocation of PKC from the cytosol to a particulate fraction (Kraft and Anderson: Nature 301: 621-623, 1983). The p isoform of PKC is translocated and degraded much more rapidly than the a isoform in phorbolester-stimulated rat basophilic leukemia (RBL) cells (Huang et al.: J. Biol. Chem. 264: 4238-4243, 1989). We report here immunofluorescence evidence that the distributions of PKC a and p are strikingly different in antigen-activated RBL cells. PKC p associates with perinuclear filaments and filaments that extend from the perinuclear area to the cell periphery whereas PKC a concentrates in regions of the cell periphery. This distribution of PKC p is distinctly different from that of actin filaments and microtubules as determined by phalloidin staining and by anti-tubulin antibody labeling. In contrast, the staining patterns obtained with antibodies to PKC p and to the intermediate filament protein vimentin are almost identical, indicating that PKC p associates with vimentin filaments. These bundles of 100 A filaments may provide docking sites for interactions of PKC p with its substrates and thus confer specificity to the actions of this isoform. 0 1992 Wiley-Liss, Inc.