Subcellular Localization of Diacylglycerol-responsive Protein Kinase C Isoforms in HeLa Cells
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Subcellular localization of protein kinase often plays an important role in determining its activity and specificity. Protein kinase C (PKC), a family of multi-gene protein kinases has long been known to be translocated to the particular cellular compartments in response to DAG or its analog phorbol esters. We used C-terminal green fluorescent protein (GFP) fusion proteins of PKC isoforms to visualize the subcellular distribution of individual PKC isoforms. Intracellular localization of PKC-GFP proteins was monitored by fluorescence microscopy after transient transfection of PKC-GFP expression vectors in the HeLa cells. In unstimulated HeLa cells, all PKC isoforms were found to be distributed throughout the cytoplasm with a few exceptions. PKCθ was mostly localized to the Golgi, and PKCγ, PKCδ and PKCη showed cytoplasmic distribution with Golgi localization. DAG analog TPA induced translocation of PKC-GFP to the plasma membrane. PKCα, PKCη and PKCθ were also localized to the Golgi in response to TPA. Only PKCδ was found to be associated with the nuclear membrane after transient TPA treatment. These results suggest that specific PKC isoforms are translocated to different intracellular sites and exhibit distinct biological effects.
|Tidskrift||Bulletin of the Korean Chemical Society|
|Status||Published - 2009 jan 31|
|Peer review utförd||Ja|
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