Rho-Kinase-Dependent Myristoylated Alanine-Rich C-Kinase Substrate Phosphorylation and Regulation of Neurofilament Structure in Neuronal Cells
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- Sasaki Yasuharu
- Department of Pharmacology, Pharmaceutical Science, Kitasato University
書誌事項
- タイトル別名
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- 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
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説明
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-β, 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.<br>
収録刊行物
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- Journal of Pharmacological Sciences
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Journal of Pharmacological Sciences 93 (1), 35-40, 2003
公益社団法人 日本薬理学会
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詳細情報 詳細情報について
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- CRID
- 1390282680153889536
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- NII論文ID
- 10011705959
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- NII書誌ID
- AA11806667
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- COI
- 1:STN:280:DC%2BD3svktFahtQ%3D%3D
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- ISSN
- 13478648
- 13478613
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- NDL書誌ID
- 6691559
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- PubMed
- 14501149
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- NDLサーチ
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- PubMed
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