2026-03-09T09:35:39Z https://tokushima-u.repo.nii.ac.jp/oai

oai:tokushima-u.repo.nii.ac.jp:02007544 2025-04-28T07:17:35Z 1713853213384:1713853296295:1716267876683:1716268551628

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 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 三宅, 一央 568 ミヤケ, カズヒサ 246750/profile-ja.html Miyake, Kazuhisa 70633345 坂根, 亜由子 328 サカネ, アユコ 174982/profile-ja.html Sakane, Ayuko 60509777 ツチヤ, ユウコ ツチヤ, ユウコ Tsuchiya, Yuko 佐川, 幾子 460 サガワ, イクコ 209932/profile-ja.html Sagawa, Ikuko トミダ, ヨウコ トミダ, ヨウコ Tomida, Yoko 笠原, 二郎 404 カサハラ, ジロウ 201603/profile-ja.html Kasahara, Jiro 10295131 井本, 逸勢 444 イモト, イッセイ 30258610 Imoto, Issei ワタナベ, シオ ワタナベ, シオ Watanabe, Shio ヒゴ, ダイスケ ヒゴ, ダイスケ Higo, Daisuke ミズグチ, ケンジ ミズグチ, ケンジ Mizuguchi, Kenji 佐々木, 卓也 489 ササキ, タクヤ 22215/profile-ja.html Sasaki, Takuya 40241278 JRAB/MICAL-L2 Actin Cytoskeleton Intramolecular interaction LIM domain 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. doctoral thesis Springer Nature 2019-09-05 NA application/pdf application/pdf Scientific Reports 9 12794 20452322 https://tokushima-u.repo.nii.ac.jp/record/2007544/files/k3359_abstract_review.pdf https://tokushima-u.repo.nii.ac.jp/record/2007544/files/k3359_fulltext.pdf https://tokushima-u.repo.nii.ac.jp/records/2007544 eng This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.