Electrophoresis, Vol.21, No.13, 2684-2687, 2000
Protein kinase C alpha-dependent phosphorylation of golgi proteins
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.