ArticleThe Journal of biological chemistry2012
Mechanism for CARMIL protein inhibition of heterodimeric actin-capping protein.
Article in The Journal of biological chemistry, 2012. 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, 35 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
- 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
- Biophysical Mechanism of Allosteric Regulation of Actin Capping Protein.Journal of molecular biology · 2023Article
- Proteomics of Plasma and Plasma-Treated Podocytes: Application to Focal and Segmental Glomerulosclerosis.International journal of molecular sciences · 2023Article
- Dual regulation of the actin cytoskeleton by CARMIL-GAP.Journal of cell science · 2022Article
- Structure and function of an atypical homodimeric actin capping protein from the malaria parasite.Cellular and molecular life sciences : CMLS · 2022Article
- The structure of the actin filament uncapping complex mediated by twinfilin.Science advances · 2021Article
- Comparative Analysis of CPI-Motif Regulation of Biochemical Functions of Actin Capping Protein.Biochemistry · 2020Article
- In vivo proximity proteomics of nascent synapses reveals a novel regulator of cytoskeleton-mediated synaptic maturation.Nature communications · 2019Article
- Article
- Allosteric Coupling of CARMIL and V-1 Binding to Capping Protein Revealed by Hydrogen-Deuterium Exchange.Cell reports · 2018Article
- CARMIL family proteins as multidomain regulators of actin-based motility.Molecular biology of the cell · 2017Article
- V-1 regulates capping protein activity in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The scaffolding function of the RLTPR protein explains its essential role for CD28 co-stimulation in mouse and human T cells.The Journal of experimental medicine · 2016Article
- Tropomodulin-3 is essential in asymmetric division during mouse oocyte maturation.Scientific reports · 2016Article
- CARMIL2 is a novel molecular connection between vimentin and actin essential for cell migration and invadopodia formation.Molecular biology of the cell · 2015Article
- Polarized Rac-dependent protrusions drive epithelial intercalation in the embryonic epidermis of C. elegans.Development (Cambridge, England) · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Capping protein (CP) controls the polymerization of actin filaments by capping their barbed ends. In lamellipodia, CP dissociates from the actin cytoskeleton rapidly, suggesting the possible existence of an uncapping factor, for which the protein CARMIL (capping protein, Arp2/3 and myosin-I linker) is a candidate. CARMIL binds to CP via two motifs. One, the CP interaction (CPI) motif, is found in a number of unrelated proteins; the other motif is unique to CARMILs, the CARMIL-specific interaction motif. A 115-aa CARMIL fragment of CARMIL with both motifs, termed the CP-binding region (CBR), binds to CP with high affinity, inhibits capping, and causes uncapping. We wanted to understand the structural basis for this function. We used a collection of mutants affecting the actin-binding surface of CP to test the possibility of a steric-blocking model, which remained open because a region of CBR was not resolved in the CBR/CP co-crystal structure. The CP actin-binding mutants bound CBR normally. In addition, a CBR mutant with all residues of the unresolved region changed showed nearly normal binding to CP. Having ruled out a steric blocking model, we tested an allosteric model with molecular dynamics. We found that CBR binding induces changes in the conformation of the actin-binding surface of CP. In addition, ∼30-aa truncations on the actin-binding surface of CP decreased the affinity of CBR for CP. Thus, CARMIL promotes uncapping by binding to a freely accessible site on CP bound to a filament barbed end and inducing a change in the conformation of the actin-binding surface of 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.