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Protein kinase C in rat brain synaptosomes
Author(s) -
Tanaka Shin-ichiro,
Tominaga Masahiro,
Yasuda Ichiro,
Kishimoto Akira,
Nishizuka Yasutomi
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81445-e
Subject(s) - protein kinase c , proteolysis , biochemistry , phosphorylation , chemistry , enzyme , calpain , threonine , protein kinase a , cyclin dependent kinase 5 , kinase , microbiology and biotechnology , biology , serine , mitogen activated protein kinase kinase
A small fraction (approximately 5%) of protein kinase C (PKC) in the adult rat brain synaptosomes is tightly associated with Triton X‐100‐insoluble components (most likely membrane‐skeleton elements), and is solubilized only after denaturation with sodium dodecyl sulfate. The kinase domain of this PKC can be released as a soluble form after limited proteolysis with calpain, whereas the regulatory domain which binds phorbol ester remains insoluble. The PKC in this fraction was identified as the βII‐subspecies or its related molecule. Presumably, this enzyme subspecies is responsible for the phosphorylation of a major PKC substrate protein, growth‐associated protein‐43, which is located in nerve endings as well as in growth cones in association with the membrane‐skeleton elements.