ArticleScientific reports2019
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.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 21 citations in OpenAlex.
- Molecules interacting with CasL-Like 2 enhances tumor angiogenesis and progression by activating mTOR/HIF1α/VEGF pathway in kidney renal clear cell carcinoma.Scientific reports · 2025Article
- Autoinhibition and relief mechanisms for MICAL monooxygenases in F-actin disassembly.Nature communications · 2024Article
- MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics.Frontiers in cell and developmental biology · 2023Review
- MICALL2 as a substrate of ubiquitinase TRIM21 regulates tumorigenesis of colorectal cancer.Cell communication and signaling : CCS · 2022Article
- Article
- Identification of MICALL2 as a Novel Prognostic Biomarker Correlating with Inflammation and T Cell Exhaustion of Kidney Renal Clear Cell Carcinoma.Journal of Cancer · 2022Article
- JRAB/MICAL-L2 undergoes liquid-liquid phase separation to form tubular recycling endosomes.Communications biology · 2021Article
- The mechanism of activation of the actin binding protein EHBP1 by Rab8 family members.Nature communications · 2020Article
- Molecular Characterization of a Novel Shell Matrix Protein With PDZ Domain FromFrontiers in physiology · 2020Article
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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