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PKC induces RhoA activation followed by phosphorylation of MARCKS and MBS in neuroblastoma SH‐SY5Y cells.
Author(s) -
Tanabe Atsuhiro,
Kamisuki Yukinori,
Negishi Manabu,
Suzuki Masaaki,
Hidaka Hiroyoshi
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a1121-c
Subject(s) - marcks , rhoa , protein kinase c , phosphorylation , microbiology and biotechnology , rho associated protein kinase , chemistry , staurosporine , bisindolylmaleimide , signal transduction , kinase , biology
Both PKC and ROCK participate in many cellular functions including smooth muscle contraction, cytokinesis, and gene expression. However, the effecters of PKC in these phenomena are not fully elucidated. Although myristoylated alanine rich C‐kinase substrate (MARCKS) is recognized as the substrate of PKC, we have previously shown that ROCK also phosphorylates S159 of MARCKS. We herein report the effects of PKC on RhoA/ROCK pathway in neuronal cells. Generally, PDBu directly activates PKC, and LPA activates both PKC and ROCK through LPA receptor. ROCK specific inhibitor H‐1152 inhibited PDBu‐induced MARCKS phosphorylation as well as LPA‐induced phosphorylation in neuroblastoma cell SH‐SY5Y. We detected in GST‐pull down assay that PDBu induced the activation of RhoA in SH‐SY5Y cells. Moreover, PDBu induced the phosphorylation of myosin binding substrate (MBS) and the phosphorylation was also blocked by H‐1152. We propose the possibility that some phenomena induced by PKC are mediated through RhoA/ROCK pathway in neuronal cells.