ISSN:
0886-1544
Keywords:
cytoskeletal localization
;
signal transduction
;
intermediate filaments
;
rat basophilic leukemia cells
;
translocation
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Medicine
Notes:
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 β isoform of PKC is translocated and degraded much more rapidly than the β 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 α and β are strikingly different in antigen-activated RBL cells. PKC β associates with perinuclear filaments and filaments that extend from the perinuclear area to the cell periphery whereas PKC β concentrates in regions of the cell periphery. This distribution of PKC β 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 β and to the intermediate filament protein vimentin are almost identical, indicating that PKC β associates with vimentin filaments. These bundles of 100 Å filaments may provide docking sites for interactions of PKC β with its substrates and thus confer specificity to the actions of this isoform. © 1992 Wiley-Liss, Inc.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/cm.970220405
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