TY - JOUR
T1 - Spatiotemporal distribution of PKCα, PIP3, Moesin, Cdc42, MARCKS, Scriblle, and Arf6 before directed cell migration in monolayers
AU - Lu, Quanzhi
AU - Ushijima, Katsuyuki
AU - Sasaki, Saori
AU - Sera, Toshihiro
AU - Takeishi, Naoki
AU - Kudo, Susumu
N1 - Publisher Copyright:
© 2025 Elsevier Inc.
PY - 2025/3/1
Y1 - 2025/3/1
N2 - Protein kinase Cα (PKCα) has an important role in directed cell migration. After a mechanical wounding, PKCα rapidly accumulates at cell edges adjacent to the wounded cell and regulates cell migration. However, the proteins downstream of PKCα that mediate directed signaling remain unknown. In this study, we examined the spatiotemporal dynamics of PKCα, PIP3, Moesin, Cdc42, MARCKS, Scribble, and Arf6 before directed migration. After wounding, PIP3, Moesin, and Cdc42 accumulated at the cell edge near the wounded cells later than PKCα. In contrast, MARCKS moved away from the plasma membrane without polarization, and Scribble and Arf6 exhibited no significant translocation. The inhibition of PIP3 suppressed the accumulation of Moesin and Cdc42, suggesting that PIP3 regulates Moesin and Cdc42. In particular, the inhibition of PKCα completely inhibited the translocation of all factors, indicating that PKCα is a central regulator in early signaling after wounding and before directional migration.
AB - Protein kinase Cα (PKCα) has an important role in directed cell migration. After a mechanical wounding, PKCα rapidly accumulates at cell edges adjacent to the wounded cell and regulates cell migration. However, the proteins downstream of PKCα that mediate directed signaling remain unknown. In this study, we examined the spatiotemporal dynamics of PKCα, PIP3, Moesin, Cdc42, MARCKS, Scribble, and Arf6 before directed migration. After wounding, PIP3, Moesin, and Cdc42 accumulated at the cell edge near the wounded cells later than PKCα. In contrast, MARCKS moved away from the plasma membrane without polarization, and Scribble and Arf6 exhibited no significant translocation. The inhibition of PIP3 suppressed the accumulation of Moesin and Cdc42, suggesting that PIP3 regulates Moesin and Cdc42. In particular, the inhibition of PKCα completely inhibited the translocation of all factors, indicating that PKCα is a central regulator in early signaling after wounding and before directional migration.
KW - Cdc42
KW - Cell migration
KW - Moesin
KW - Myristoylated alanine-rich C kinase substrate
KW - Phosphatidylinositol 3,4,5-triphosphate
KW - Protein kinase Cα
UR - http://www.scopus.com/inward/record.url?scp=85216467875&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2025.151371
DO - 10.1016/j.bbrc.2025.151371
M3 - Article
C2 - 39892054
AN - SCOPUS:85216467875
SN - 0006-291X
VL - 750
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
M1 - 151371
ER -