Actin Cytoskeletal Reorganization Function of JRAB/MICAL-L2 Is Fine-tuned by Intramolecular Interaction between First LIM Zinc Finger and C-terminal Coiled-coil Domains

• Material Type: 博士論文
• ISSN: 2045-2322
• Title: Actin Cytoskeletal Reorganization Function of JRAB/MICAL-L2 Is Fine-tuned by Intramolecular Interaction between First LIM Zinc Finger and C-terminal Coiled-coil Domains
• Volume: 9
• Author/Editor: Miyake, Kazuhisa; Sakane, Ayuko; Tsuchiya, Yuko; Sagawa, Ikuko; Tomida, Yoko; Kasahara, Jiro; Imoto, Issei; Watanabe, Shio; Higo, Daisuke; Mizuguchi, Kenji; Sasaki, Takuya
• Author Heading: Miyake, Kazuhisa; Sakane, Ayuko; Tsuchiya, Yuko; Sagawa, Ikuko; Tomida, Yoko; Kasahara, Jiro; Imoto, Issei; Watanabe, Shio; Higo, Daisuke; Mizuguchi, Kenji; Sasaki, Takuya
• Publication, Distribution, etc.: Springer Nature
• Publication Date: 2019-09-05
• Publication Date (W3CDTF): 2019-09-05
• Alternative Title: 分子内結合が調節するJRABのLIMドメインによるアクチン細胞骨格の再編成
• Periodical title: Scientific Reports
• Degree grantor/type: 徳島大学
• Date Granted: 2020-02-27
• Date Granted (W3CDTF): 2020-02-27
• Dissertation Number: 甲第3359号
• Degree Type: 博士（医学）
• Conferring No. (Dissertation): 甲第3359号
• Text Language Code: eng
• Subject Heading: JRAB/MICAL-L2; Actin Cytoskeleton; Intramolecular interaction; LIM domain
• Target Audience: 一般
• Note (General): JRAB/MICAL-L2 is an effector protein of Rab13, a member of the Rab family of small GTPase. JRAB/MICAL-L2 consists of a calponin homology domain, a LIM domain, and a coiled-coil domain. JRAB/MICAL-L2 engages in intramolecular interaction between the N-terminal LIM domain and the C-terminal coiled-coil domain, and changes its conformation from closed to open under the effect of Rab13. Open-form JRAB/MICAL-L2 induces the formation of peripheral ruffles via an interaction between its calponin homology domain and filamin. Here, we report that the LIM domain, independent of the C-terminus, is also necessary for the function of open-form JRAB/MICAL-L2. In mechanistic terms, two zinc finger domains within the LIM domain bind the first and second molecules of actin at the minus end, potentially inhibiting the depolymerization of actin filaments (F-actin). The first zinc finger domain also contributes to the intramolecular interaction of JRAB/MICAL-L2. Moreover, the residues of the first zinc finger domain that are responsible for the intramolecular interaction are also involved in the association with F-actin. Together, our findings show that the function of open-form JRAB/MICAL-L2 mediated by the LIM domain is fine-tuned by the intramolecular interaction between the first zinc finger domain and the C-terminal domain.
• DOI: info:doi/10.1038/s41598-019-49232-8; https://doi.org/info:doi/10.1038/s41598-019-49232-8
• Persistent ID (NDL): info:ndljp/pid/11490367; https://dl.ndl.go.jp/pid/11490367
• Collection: 障害者向け資料
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• Collection (particular): 国立国会図書館デジタルコレクション > デジタル化資料 > 博士論文; https://dl.ndl.go.jp/collections/A00014
• Acquisition Basis: 博士論文（自動収集）
• Date Accepted (W3CDTF): 2020-05-25T09:38:44+09:00
• Format (IMT): application/pdf
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• Periodical Title (URI): http://repo.lib.tokushima-u.ac.jp/114610
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