Abstract
Protein kinase D (PKD) binds to diacylglycerol (DAG) in the trans-Golgi network (TGN) and is activated by trimeric G-protein subunits beta gamma. This complex then regulates the formation of transport carriers in the TGN that traffic to the plasma membrane in non-polarized cells. Here we report specificity of different PKD isoforms in regulating protein trafficking from the TGN. Kinase-inactive forms of PKD1, PKD2 and PKD3 localize to the TGN in polarized and non-polarized cells. PKD activity is required only for the transport of proteins containing basolateral sorting information, and seems to be cargo specific.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Cell Line
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Cell Polarity
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Diglycerides / metabolism
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Dogs
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Epithelial Cells / cytology
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Epithelial Cells / metabolism
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HeLa Cells
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Humans
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Isoenzymes / metabolism
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Protein Kinase C / genetics
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Protein Kinase C / metabolism*
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Protein Kinase D2
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Protein Kinases / genetics
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Protein Kinases / metabolism*
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Protein Transport / physiology
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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trans-Golgi Network / metabolism*
Substances
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Diglycerides
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Isoenzymes
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Protein Kinase D2
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Recombinant Fusion Proteins
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Protein Kinases
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protein kinase C nu
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protein kinase D
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Protein Kinase C