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- W2053065294 abstract "Myristoylated alanine-rich C-kinase substrate (MARCKS) is an actin-binding protein whose function may be regulated by the phosphorylation of multiple sites, in which the phosphorylation site domain (PSD) is recognized to have three or four PKC-dependent sites. Recently, it is considered that MARCKS is implicated in some neuronal functions, such as synaptic vesicle trafficking and neurotransmitter release, through regulation of the actin-containing cytoskeletal structure; this is based on the experimental results with short-term or prolonged pretreatment with phorbol esters and treatment by protein kinase C (PKC) inhibitor. However, the precise molecular mechanism is yet obscure. Recently, we have demonstrated that MARCKS is phosphorylated at Ser159 in PSD by Rho-kinase in vitro and that the phosphorylation occurred in neuronal cells upon stimulation with lysophosphatidic acid (LPA), and its phosphorylation was inhibited by a novel and specific Rho-kinase inhibitor, H-1152. Our results allow us to speculate that a preinflammatory substance, such as LPA, interleukin 1-beta, and bradykinin, augments MARCKS phosphorylation in a novel signal transduction pathway besides the PKC-involved one, and thereby induces the release of a neurotransmitter through a reorganization of actin-containing microfilaments at the cell periphery, the so-called active zone. In this section, I address a novel mechanism for MARCKS phosphorylation and its related cellular function." @default.
- W2053065294 created "2016-06-24" @default.
- W2053065294 creator A5060725150 @default.
- W2053065294 date "2003-01-01" @default.
- W2053065294 modified "2023-09-25" @default.
- W2053065294 title "New Aspects of Neurotransmitter Release and Exocytosis: Rho-Kinase-Dependent Myristoylated Alanine-Rich C-Kinase Substrate Phosphorylation and Regulation of Neurofilament Structure in Neuronal Cells" @default.
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- W2053065294 doi "https://doi.org/10.1254/jphs.93.35" @default.
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