Abstract
Golgi-enriched membranes were phosphorylated in order to understand the mechanism for protein kinase C (PKC) regulation of exocytic vesicle formation at the trans-Golgi network. Two of the main PKC substrates were identified as MARCKS and Mac-MARCKS by two-dimensional electrophoresis (2-DE) and mass spectrometric sequencing. Annexin IV and profilin I, two other Golgi-associated proteins--although known as in vitro PKC substrates--were not phosphorylated in the Golgi-bound state.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Annexin A4 / metabolism
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Blotting, Western
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Calmodulin-Binding Proteins
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Carcinoma, Hepatocellular / metabolism
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Carcinoma, Hepatocellular / pathology
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Contractile Proteins*
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Electrophoresis, Gel, Two-Dimensional
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Golgi Apparatus / metabolism*
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Humans
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Intracellular Signaling Peptides and Proteins*
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Isoenzymes / physiology*
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Liver Neoplasms / metabolism
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Liver Neoplasms / pathology
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Membrane Proteins / metabolism*
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Microfilament Proteins / metabolism
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Myristoylated Alanine-Rich C Kinase Substrate
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Neoplasm Proteins / metabolism
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Phosphorylation
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Profilins
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Protein Kinase C / physiology*
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Protein Kinase C-alpha
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Protein Processing, Post-Translational*
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Proteins / metabolism*
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R-SNARE Proteins
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Spectrometry, Mass, Electrospray Ionization
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Substrate Specificity
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Tumor Cells, Cultured / metabolism
Substances
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Annexin A4
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Calmodulin-Binding Proteins
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Contractile Proteins
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Intracellular Signaling Peptides and Proteins
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Isoenzymes
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MARCKS protein, human
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MARCKSL1 protein, human
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Membrane Proteins
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Microfilament Proteins
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Neoplasm Proteins
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PFN1 protein, human
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Profilins
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Proteins
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R-SNARE Proteins
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VAMP8 protein, human
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Myristoylated Alanine-Rich C Kinase Substrate
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PRKCA protein, human
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Protein Kinase C
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Protein Kinase C-alpha