TY - JOUR
T1 - Selective interaction of protein kinase F(A)/glycogen synthase kinase-3α with membrane phospholipids
AU - Yu, Jau Song
AU - Chan, Wen Hsiung
AU - Yang, Shiaw Der
PY - 1997/8/18
Y1 - 1997/8/18
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0031577485&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1997.7147
DO - 10.1006/bbrc.1997.7147
M3 - 文章
C2 - 9268710
AN - SCOPUS:0031577485
SN - 0006-291X
VL - 237
SP - 331
EP - 335
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -