Selective interaction of protein kinase F(A)/glycogen synthase kinase-3α with membrane phospholipids

Jau Song Yu*, Wen Hsiung Chan, Shiaw Der Yang

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

3 Scopus citations

Abstract

Previously we reported that the activity of protein kinase F(A)/glycogen synthase kinase-3α (kinase F(A)/GSK-3α) can be detected in several brain membrane fractions. In this report, we examined whether kinase F(A)/GSK-3α can directly interact with membrane phospholipids by using anti-kinase F(A)/GSK-3α antibody as a more specific studying tool. It was found that kinase F(A)/GSK-3α can associate with NaOH-extracted brain membranes and selectively interact with several kinds of reconstituted phospholipid vesicles including phosphatidic acid (PA), phosphatidyl ethanolamine (PE), phosphatidyl inositol (PI), and phosphatidyl serine (PS) vesicles. Increasing ionic strength in the reaction could disrupt the interaction between kinase F(A)/GSK-3α and PA, PI, or PE vesicles but had no effect on the interaction between kinase F(A)/GSK-3α and PS vesicles, indicating that both ionic and non-ionic interactions are involved in this process, respectively. Moreover, both kinase activity and protease sensitivity of kinase F(A)/GSK-3α can be affected profoundly by these phospholipid vesicles and different forms of the kinase can be produced when it binds to distinct types of phospholipid vesicles. Taken together, the results demonstrate a direct interaction of kinase F(A)/GSK-3α with membrane phospholipids and suggest that membrane phospholipids may be directly involved in regulating kinase F(A)/GSK-3α activity.

Original languageEnglish
Pages (from-to)331-335
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume237
Issue number2
DOIs
StatePublished - 18 08 1997

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