ArticleThe Journal of biological chemistry2016
Cell Migration and Invadopodia Formation Require a Membrane-binding Domain of CARMIL2.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 33 citations in OpenAlex.
- CARMIL membrane-binding domain regulates capping protein and actin assembly.The Journal of biological chemistry · 2026Article
- Mechanisms of CARMIL dimerization, autoinhibition, and capping protein binding.Science advances · 2026Article
- Coordinated regulation of Capping Protein by CARMIL and V-1/myotrophin.The Journal of biological chemistry · 2026Review
- β-Actin Deficiency in Baraitser-Winter Syndrome Type 1 Disrupts T-Cell Function and Immune Regulation: Implications for Targeted Therapy in Actinopathies.Journal of clinical immunology · 2025Article
- Reconstitution of Arp2/3-nucleated actin assembly with proteins CP, V-1, and CARMIL.Current biology : CB · 2024Article
- Reconstitution of Arp2/3-Nucleated Actin Assembly with CP, V-1 and CARMIL.bioRxiv : the preprint server for biology · 2024Article
- Novel CARMIL2 (RLTPR) Mutation Presenting with Hyper-IgE and Eosinophilia: A Case Report.Endocrine, metabolic & immune disorders drug targets · 2024Article
- Biophysical Mechanism of Allosteric Regulation of Actin Capping Protein.Journal of molecular biology · 2023Article
- High spatial-resolved heat manipulating membrane heterogeneity alters cellular migration and signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- CARMIL3 is important for cell migration and morphogenesis during early development in zebrafish.Developmental biology · 2022Article
- Case report: Primary immunodeficiency due to a novel mutation in CARMIL2 and its response to combined immunomodulatory therapy.Frontiers in pediatrics · 2022Article
- Bronchopleural fistula in a 5- years old child with novel CARMIL 2 mutation: A rare disease and a rare case.Annals of medicine and surgery (2012) · 2021Article
- Novel CARMIL2 loss-of-function variants are associated with pediatric inflammatory bowel disease.Scientific reports · 2021Article
- Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Nature cell biology · 2021Article
- The structure of the actin filament uncapping complex mediated by twinfilin.Science advances · 2021Article
- High expression of CIN85 promotes proliferation and invasion of human esophageal squamous cell carcinoma.Molecular medicine reports · 2021Article
- Comparative Analysis of CPI-Motif Regulation of Biochemical Functions of Actin Capping Protein.Biochemistry · 2020Article
- Complex Muco-cutaneous Manifestations of CARMIL2-associated Combined Immunodeficiency: A Novel Presentation of Dysfunctional Epithelial Barriers.Acta dermato-venereologica · 2020Article
- Basic-hydrophobic sites are localized in conserved positions inside and outside of PH domains and affect localization ofMolecular biology of the cell · 2020Article
- Low-dose tubacin promotes BMSCs proliferation and morphological changes through the ERK pathway.American journal of translational research · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
CARMILs regulate capping protein (CP), a critical determinant of actin assembly and actin-based cell motility. Vertebrates have three conserved CARMIL genes with distinct functions. In migrating cells, CARMIL2 is important for cell polarity, lamellipodial assembly, ruffling, and macropinocytosis. In cells, CARMIL2 localizes with a distinctive dual pattern to vimentin intermediate filaments and to membranes at leading edges and macropinosomes. The mechanism by which CARMIL2 localizes to membranes has not been defined. Here, we report that CARMIL2 has a conserved membrane-binding domain composed of basic and hydrophobic residues, which is necessary and sufficient for membrane localization, based on expression studies in cells and on direct binding of purified protein to lipids. Most important, we find that the membrane-binding domain is necessary for CARMIL2 to function in cells, based on rescue expression with a set of biochemically defined mutants. CARMIL1 and CARMIL3 contain similar membrane-binding domains, based on sequence analysis and on experiments, but other CPI motif proteins, such as CD2AP, do not. Based on these results, we propose a model in which the membrane-binding domain of CARMIL2 tethers this multidomain protein to the membrane, where it links dynamic vimentin filaments with regulation of actin assembly via CP.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.