Abstract
Protein kinase D (PKD) is recruited to the trans-Golgi network (TGN) through interaction with diacylglycerol (DAG) and is required for the biogenesis of TGN to cell surface transport carriers. We now provide definitive evidence that PKD has a function in membrane fission. PKD depletion by siRNA inhibits trafficking from the TGN, whereas expression of a constitutively active PKD converts TGN into small vesicles. These findings demonstrate that PKD regulates membrane fission and this activity is used to control the size of transport carriers, and to prevent uncontrolled vesiculation of TGN during protein transport.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Biological Transport / physiology
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Dimerization
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HeLa Cells
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Humans
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Intracellular Membranes / metabolism*
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Intracellular Membranes / ultrastructure
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Phosphorylation
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Protein Isoforms / antagonists & inhibitors
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Protein Isoforms / metabolism
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Protein Isoforms / physiology
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Protein Kinase C / antagonists & inhibitors
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Protein Kinase C / metabolism
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Protein Kinase C / physiology*
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Protein Kinase D2
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Protein Kinases / metabolism
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Protein Kinases / physiology
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RNA Interference
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Transport Vesicles / metabolism*
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Transport Vesicles / ultrastructure
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trans-Golgi Network / physiology*
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trans-Golgi Network / ultrastructure
Substances
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Protein Isoforms
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Protein Kinase D2
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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