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Protein kinase Cα‐dependent phosphorylation of Golgi proteins
Author(s) -
Radau Boris,
Otto Albrecht,
Müller EvaChristina,
Westermann Peter
Publication year - 2000
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(20000701)21:13<2684::aid-elps2684>3.0.co;2-g
Subject(s) - golgi apparatus , protein kinase c , marcks , microbiology and biotechnology , phosphorylation , chemistry , protein kinase a , kinase , secretion , biochemistry , biology , endoplasmic reticulum
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 MacMARCKS 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.