Affinage

CARMIL1

F-actin-uncapping protein LRRC16A · UniProt Q5VZK9

Length
1371 aa
Mass
151.6 kDa
Annotated
2026-04-28
35 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CARMIL1 is a large multidomain scaffold protein that coordinates actin barbed-end dynamics, membrane protrusion, and signaling at the leading edge of migrating cells. It dimerizes via a central helical domain and localizes to the plasma membrane through a non-canonical PH domain; its C-terminal CAH3/CBR domain allosterically inhibits capping protein (CP) and directly uncaps CP-capped actin filament barbed ends—reducing CP barbed-end half-life from ~30 min to ~10 s—thereby converting V-1-sequestered inactive CP into weakly capping CP:CARMIL complexes that promote Arp2/3-dependent actin network assembly at membrane protrusion sites (PMID:19926785, PMID:24778263, PMID:39437783). An intramolecular 'antenna' motif connecting the helical domain to the CBR contacts the LRR dimer interface and mediates partial autoinhibition, while the LRR domain independently engages IL-1R1/IRAK to support IL-1-induced ERK signaling and associates with the Rac GEF Trio to activate Rac1, collectively driving lamellipodia formation, macropinocytosis, and cell migration (PMID:41861019, PMID:32610117, PMID:19846667, PMID:39602282).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2001 High

    Identification of CARMIL as a physical hub linking capping protein, Arp2/3 complex, and type I myosins established that a single scaffold coordinates barbed-end capping, actin nucleation, and motor-driven membrane dynamics, and that its loss impairs macropinocytosis and chemotaxis.

    Evidence SH3-domain pulldown, co-IP, Arp2/3 nucleation assay, and p116-null Dictyostelium phenotypic analysis

    PMID:11425877

    Open questions at the time
    • Mammalian ortholog function unknown
    • Direct binding affinities not measured
    • Mechanism of CP regulation (inhibition vs. uncapping) not resolved
  2. 2003 High

    Quantitative biophysical characterization revealed that CARMIL self-associates as a monomer-dimer equilibrium and binds CP with submicromolar affinity through a C-terminal proline-rich region, establishing the basic architecture and stoichiometry of the CARMIL-CP complex.

    Evidence Analytical ultracentrifugation, surface plasmon resonance, rotary-shadow EM of Acanthamoeba CARMIL

    PMID:14594951

    Open questions at the time
    • Binding mechanism (steric vs. allosteric) unresolved
    • Mammalian CARMIL not yet characterized
  3. 2005 High

    Transfer of CARMIL function to mammalian cells showed that CARMIL1 concentrates in lamellipodia, anti-caps CP to promote barbed-end polymerization, and is required for lamellipodial protrusion and cell migration—establishing its conserved role in mammalian cell motility.

    Evidence In vitro barbed-end capping assay, siRNA knockdown with full-length vs. CP-binding-deficient rescue in cultured cells

    PMID:16054028

    Open questions at the time
    • Uncapping activity not directly demonstrated
    • Membrane-targeting mechanism unknown
    • Rac1 connection not yet established
  4. 2006 High

    Mapping the minimal anti-capping and uncapping activity to the conserved CAH3 domain, and showing that full-length CARMIL is partially autoinhibited, defined the functional module within the multidomain protein and introduced the concept of intramolecular regulation.

    Evidence In vitro reconstituted capping/uncapping assays with GST-fusion domain deletions and point mutants

    PMID:16434392

    Open questions at the time
    • Structural basis of autoinhibition unknown
    • Mechanism of uncapping (steric vs. allosteric) unresolved
  5. 2009 High

    Multiple advances resolved CARMIL1's uncapping mechanism, membrane association, and signaling connections: single-molecule TIRF showed CAH3 physically removes CP from barbed ends reducing its dwell time from ~30 min to ~10 s; lipid-binding sites were mapped; and CARMIL1 was linked to Rac1 activation via Trio, while C. elegans genetics placed CARMIL upstream of Trio in guidance signaling.

    Evidence Single-molecule TIRF of mGFP-CP uncapping; peptide-lipid vesicle binding; siRNA knockdown with Rac1 pull-down and co-IP of Trio; C. elegans genetic epistasis and in vivo co-IP

    PMID:19244282 PMID:19846667 PMID:19926785 PMID:20018884

    Open questions at the time
    • Atomic-resolution structure of full-length CARMIL unavailable
    • Whether CARMIL activates or inhibits Trio GEF activity unclear across species
    • Lipid specificity and PH domain structure not resolved
  6. 2010 High

    NMR structural analysis of the CAH3-CP interface revealed that CAH3a binds an acidic groove on CP opposite its actin-binding surface and positions CAH3b near CP's basic patch, providing the first atomic model explaining how CARMIL disrupts CP-barbed-end interaction without occupying the actin-binding site.

    Evidence NMR solution structure of CAH3-CP complex with confirmatory mutagenesis

    PMID:20630878

    Open questions at the time
    • Whether uncapping proceeds by allosteric or steric mechanism still debated
    • Full-length structural context missing
  7. 2012 High

    Ruling out steric blockade and demonstrating that CBR binding induces conformational changes in CP's actin-binding surface established that CARMIL inhibits and uncaps CP via an allosteric mechanism; the CSI motif was identified as essential for high-affinity binding and uncapping.

    Evidence CP actin-binding surface mutants retaining CBR binding; molecular dynamics simulations

    PMID:22411988

    Open questions at the time
    • Experimental demonstration of allosteric conformational change (e.g., HDX-MS) not yet performed
    • Role of CSI motif in vivo not tested
  8. 2013 High

    Crystal structure of CARMIL1 N-terminal half revealed a non-canonical PH domain and 16-repeat LRR domain; SAXS showed the helical domain mediates antiparallel dimerization positioning PH domains for membrane binding. Separately, a CP-binding point mutant (CARMIL1-AA) dissected CP-dependent (lamellipodia, macropinocytosis) from CP-independent (membrane localization, Rac1 activation, wound migration) functions.

    Evidence X-ray crystallography, SAXS, GFP imaging with PH-deletion mutants; siRNA rescue with CARMIL1-AA point mutant

    PMID:23904264 PMID:24071777

    Open questions at the time
    • Structure of C-terminal CBR-containing region unresolved
    • Identity of LRR-binding partners unknown
    • Autoinhibition mechanism structurally undefined
  9. 2014 High

    Demonstrating that CARMIL retrieves CP from the inhibitory CP:V-1 complex to generate weakly capping CP:CARMIL complexes at protrusion sites established a spatially restricted regulatory cycle explaining how inactive cytoplasmic CP is converted to a functional form specifically at the leading edge to support Arp2/3-dependent actin assembly.

    Evidence Stopped-flow kinetics, analytical ultracentrifugation, in vitro actin polymerization, live-cell TIRF of CARMIL recruitment

    PMID:24778263

    Open questions at the time
    • Reconstitution with all components on a membrane not yet achieved
    • In vivo concentrations and fluxes of CP, V-1, and CARMIL not measured
  10. 2018 High

    HDX-MS experimentally confirmed allosteric coupling between the CARMIL-binding site and CP's distal actin-binding β-tentacle, providing direct biophysical evidence for the long-range conformational changes underlying CARMIL-mediated uncapping.

    Evidence Hydrogen-deuterium exchange mass spectrometry of CP alone and in complex with CARMIL peptide and V-1

    PMID:29847807

    Open questions at the time
    • Full-length CARMIL-CP structural model still lacking
    • Dynamics of allosteric change at single-molecule resolution not captured
  11. 2019 High

    Discovery that the LRR domain of CARMIL1 associates with IL-1R1 and IRAK and is required for IL-1-induced ERK activation and MMP3 expression revealed a signaling function for CARMIL1 beyond actin regulation, linking it to inflammatory pathways.

    Evidence Tandem mass tag MS, co-IP with LRR-deletion mutants, CRISPR-Cas9 knockout, TAT-peptide competition in chondrocytes

    PMID:32610117

    Open questions at the time
    • Whether CARMIL1 is a direct scaffold vs. indirect adapter for IRAK unclear
    • Relevance to in vivo inflammatory disease not tested
  12. 2022 High

    Identification of a Dictyostelium CARMIL isoform with intrinsic Rac GAP activity demonstrated that CARMIL proteins can directly regulate Rho-family GTPases, and that both GAP and CP-regulatory activities are independently required for phagocytosis and chemotaxis.

    Evidence In vitro GTPase assay, genetic null rescue with GAP-dead and CP-regulation-deficient mutants in Dictyostelium

    PMID:35583107

    Open questions at the time
    • Mammalian CARMIL1 lacks a GAP domain; whether it regulates Rac through an analogous direct mechanism is unknown
    • Structural basis of GAP domain insertion not resolved
  13. 2024 High

    Full reconstitution on lipid-coated beads with purified Arp2/3 activator, Arp2/3, V-1, CP, profilin, and CARMIL demonstrated that membrane-anchored CARMIL counteracts V-1 inhibition and activates CP for Arp2/3-nucleated actin assembly, and that CP-binding by CARMIL1 is specifically required for macropinocytosis but dispensable for proliferation and autophagy.

    Evidence Reconstitution on lipid-coated beads with pyrene-actin assay; CRISPR-Cas9 KO cells with CARMIL1-AA rescue and macropinocytosis/autophagy assays

    PMID:39437783 PMID:39602282

    Open questions at the time
    • Reconstitution lacks Trio/Rac module
    • Contribution of CARMIL membrane release to in vivo dynamics not tested
  14. 2026 High

    Cryo-EM/crystal structures of dimeric CP-bound CARMIL1(1–1046) revealed the full-length architecture including an 'antenna' motif mediating autoinhibition at the LRR dimer interface, and reconstitution showed that the membrane-binding domain targets CPI/CSI motifs to membranes and that upon CP binding, CARMIL can release from the membrane to enhance cytoplasmic uncapping—establishing a dual-mode mechanism.

    Evidence Crystal structure of dimeric CARMIL1-CP complex; mutagenesis of antenna with in vitro uncapping and cell area assays; lipid-coated bead reconstitution with MB domain deletions

    PMID:41861019 PMID:42031174

    Open questions at the time
    • Dynamic structural transitions during membrane release not captured in real time
    • How autoinhibition is relieved by upstream signals in vivo remains unclear
    • Structure of the proline-rich/myosin-I-binding C-terminal tail still missing

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: how CARMIL1 autoinhibition is relieved by physiological signals; how LRR-mediated IL-1R1/IRAK and Trio interactions are coordinated with CP regulation at the leading edge; and whether the membrane-release uncapping mode operates in vivo during protrusion cycles.
  • No upstream activating signal for autoinhibition relief identified
  • Spatial and temporal coordination of CP-regulatory and signaling functions not resolved in vivo
  • Complete reconstitution including Trio/Rac module and myosin-I not achieved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 8 GO:0008092 cytoskeletal protein binding 6 GO:0008289 lipid binding 3 GO:0060090 molecular adaptor activity 3
Localization
GO:0005886 plasma membrane 6 GO:0005829 cytosol 1
Pathway
R-HSA-1500931 Cell-Cell communication 3 R-HSA-162582 Signal Transduction 2 R-HSA-168256 Immune System 1
Partners
ACTR2CAPZA1CAPZBIL1R1IRAK1MYO1BTRIM27TRIO
Complex memberships
CARMIL1 homodimerCP:CARMIL1 complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 Dictyostelium CARMIL (p116) physically links type I myosins (myoB, myoC), capping protein (CP alpha/beta), and the Arp2/3 complex into a single in vivo complex: myosins bind CARMIL through their SH3 domains, and CP and Arp2/3 complex bind to CARMIL's N-terminal region; a region containing an acidic stretch activates Arp2/3-dependent actin nucleation. Cells lacking p116 show defective macropinocytosis, reduced pinocytosis, impaired chemotaxis, and decreased F-actin content. SH3-domain pulldown, co-immunoprecipitation, fusion-protein binding assays, Arp2/3 nucleation assay, p116-null cell phenotypic analysis The Journal of cell biology High 11425877
2003 Acanthamoeba CARMIL binds capping protein (CP) with a Kd of ~0.4 µM via its C-terminal ~200-residue proline-rich domain; CARMIL self-associates in a monomer-dimer equilibrium (Ka ~1×10^6 M^-1) and is asymmetric, as shown by analytical ultracentrifugation and rotary-shadow EM. Co-purification, chemical cross-linking, analytical ultracentrifugation, surface plasmon resonance, SH3-domain pulldown, rotary-shadow electron microscopy The Journal of biological chemistry High 14594951
2005 Mammalian CARMIL (mCARMIL/CARMIL1) binds CP with high affinity and reduces CP's affinity for actin filament barbed ends (anti-capping activity); addition to cell extracts enhances Arp2/3- and spectrin-actin-seed-induced polymerization. In cells, mCARMIL concentrates in lamellipodia; siRNA knockdown decreases F-actin and slows cell migration via reduced lamellipodial protrusion, a phenotype rescued by full-length but not CP-binding-deficient mCARMIL. In vitro barbed-end capping assay, actin polymerization assay with cell extracts, GFP localization, siRNA knockdown with rescue Developmental cell High 16054028
2006 The conserved C-terminal CAH3 domain of CARMIL is necessary and sufficient for potent anti-capping protein activity: it inhibits CP's barbed-end capping activity and drives uncapping of CP-capped filaments. Point mutations in conserved CAH3 residues abolish these activities. Full-length CARMIL is partially autoinhibited relative to C-terminal fragments. In vitro actin polymerization/uncapping assays, GST-fusion protein binding, site-directed mutagenesis, proteolytic cleavage The Journal of biological chemistry High 16434392
2009 CARMIL1 localizes to lamellipodia and macropinosomes; CARMIL1 knockdown causes loss of lamellipodial actin, defects in protrusion/ruffling/macropinocytosis, and loss of Rac1 activation. CARMIL1 co-immunoprecipitates with the dual-GEF Trio. CARMIL2 colocalizes with vimentin intermediate filaments and loss decreases myosin-IIB levels, causing a multipolar phenotype. The two isoforms have distinct, non-redundant functions. siRNA knockdown, GFP localization, co-immunoprecipitation with Trio, Rac1 activation assay, rescue experiments Molecular biology of the cell High 19846667
2009 C. elegans CARMIL ortholog (CRML-1) negatively regulates neuronal cell and axon growth cone migration by inhibiting the Rac GEF activity of UNC-73/Trio; CRML-1 and UNC-73 form a complex in vivo, and the antagonism between them controls SAX-3/Robo guidance receptor levels. Genetic epistasis (suppressor screens, double mutants), co-immunoprecipitation in vivo Development (Cambridge, England) High 19244282
2009 CARMIL contains unstructured membrane-binding sites with basic and hydrophobic amino acid character; synthetic peptides and protein domains containing these sites bind acidic phospholipids in vitro. Peptide synthesis, lipid vesicle binding assay, computational hydrophobicity analysis The Journal of biological chemistry Medium 20018884
2009 Direct single-molecule TIRF microscopy demonstrates that the isolated CAH3 domain of mouse CARMIL-1 (mCAH3) physically removes mGFP-tagged CP from individual capped actin filament barbed ends (uncapping), reducing CP half-life at the barbed end from ~30 min to ~10 s at saturating mCAH3; the CP:CAH3 complex retains weak barbed-end affinity. Total internal reflection fluorescence microscopy (TIRF/TIRFM), single-molecule imaging, mGFP-tagged CP The Journal of biological chemistry High 19926785
2010 NMR structural analysis shows the highly basic CAH3a subdomain of mouse CARMIL-1 binds an 'acidic groove' on CP opposite its actin-binding surface, orienting CAH3b adjacent to the basic patch of CP required for barbed-end interaction; mutagenesis of both proteins confirmed specific residue contacts and provided a mechanistic explanation for uncapping. NMR (solution structure), site-directed mutagenesis, actin polymerization/uncapping assays The Journal of biological chemistry High 20630878
2012 CARMIL inhibits CP via an allosteric mechanism: molecular dynamics shows CBR binding induces conformational changes in CP's actin-binding surface; a steric-blocking model was ruled out because CP actin-binding mutants still bind CBR normally. The CARMIL-specific interaction (CSI) motif in the CP-binding region is required for high-affinity binding and uncapping. Mutagenesis of CP actin-binding surface, CP-CBR binding assays, molecular dynamics simulation The Journal of biological chemistry High 22411988
2013 Crystal structure of CARMIL1-668 reveals an N-terminal non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat (LRR) domain; small-angle X-ray scattering shows the central helical domain mediates antiparallel dimerization, positioning PH domains for simultaneous membrane interaction. Deletion of the PH domain in cells impairs leading-edge localization. X-ray crystallography, SAXS, lipid-binding assays, GFP cell imaging with deletion mutants Nature communications High 24071777
2013 The CARMIL1-CP interaction is required for lamellipodia assembly, ruffle formation, and macropinocytosis, but is dispensable for CARMIL1 membrane localization, Rac1 activation, and wound-healing cell migration, as demonstrated by a point mutant (CARMIL1-AA) that specifically disrupts CP binding. Point mutagenesis, siRNA knockdown with rescue, Rac1 activation assay, phalloidin staining, live-cell imaging Molecular biology of the cell High 23904264
2014 CARMIL retrieves CP from the inactive CP:V-1 complex via complex exchange, generating a CP:CARMIL complex with moderate (weak) barbed-end capping activity; CARMIL is recruited only to the plasma membrane at actively protruding cell edges, suggesting a spatially restricted regulatory cycle where V-1-sequestered CP is converted to weakly capping CP:CARMIL complexes specifically at protrusion sites to promote Arp2/3-dependent actin network assembly. In vitro actin polymerization assays, stopped-flow kinetics, quantitative analytical ultracentrifugation, live-cell TIRF imaging of CARMIL recruitment Proceedings of the National Academy of Sciences of the United States of America High 24778263
2018 Hydrogen-deuterium exchange mass spectrometry (HDX-MS) shows that both V-1 and CARMIL binding to CP induce changes in structural dynamics at their respective binding sites on CP and at the CP ββ subunit 'tentacle', a second distal actin-binding site, demonstrating allosteric coupling between CP modulator and actin binding sites. Hydrogen-deuterium exchange mass spectrometry (HDX-MS) Cell reports High 29847807
2019 The leucine-rich repeat (LRR) region of CARMIL1 associates with IL-1 receptor type 1 (IL-1R1) and IL-1 receptor-associated kinase (IRAK), as shown by co-immunoprecipitation with CARMIL1 LRR-deletion mutants. CARMIL1 knockout (CRISPR-Cas9) reduces IL-1-induced ERK activation by 72% and MMP3 expression by 40%; a cell-permeable TAT-CARMIL1 LRR peptide reduces collagen degradation by 43%. Tandem mass tag mass spectrometry, co-immunoprecipitation with domain mutants, CRISPR-Cas9 knockout, TAT-peptide competition, ERK phosphorylation assay Cell reports High 32610117
2022 Dictyostelium CARMIL-GAP, a CARMIL isoform with a GAP domain insert, binds Dictyostelium Rac1a and accelerates its GTP hydrolysis rate; CARMIL-GAP-null cells show defects in phagocytosis and chemotactic streaming rescued by full-length but not GAP-activity-deficient or CP-regulation-deficient versions, demonstrating that both GAP and CP-regulatory activities are required. GTPase assay (in vitro), genetic null cells, rescue with domain mutants, fluorescence localization Journal of cell science High 35583107
2024 CARMIL at a membrane surface (reconstituted with lipid-coated beads) promotes and enhances Arp2/3-nucleated actin assembly by counteracting V-1 inhibition of CP, effectively activating CP at the membrane surface for Arp2/3-mediated assembly; this reconstitution used purified Arp2/3 activator, Arp2/3 complex, V-1, CP, profilin, and actin. In vitro reconstitution with purified proteins on lipid-coated beads, pyrene-actin polymerization assay Current biology : CB High 39437783
2024 CARMIL1-AA (CP-binding mutant) selectively inhibits macropinocytosis without affecting proliferation, Rac1 activation, or autophagy, confirming that the CARMIL1-CP interaction is specifically required for macropinocytosis but not these other cellular processes. CRISPR-Cas9 knockout, expression of CARMIL1-AA point mutant, macropinocytosis assay, autophagy assay, Rac1 activation assay Molecular biology of the cell High 39602282
2024 CARMIL1 binds TRIM27 (co-immunoprecipitation), which in turn binds p53, and CARMIL1 promotes p53 degradation through TRIM27; CARMIL1 knockdown reduces ERK and mTOR phosphorylation in liver cancer cells. Co-immunoprecipitation, western blotting, siRNA knockdown, subcutaneous tumor model International immunopharmacology Medium 38739978
2026 Cryo-EM/crystal structure of CP-bound CARMIL1(1-1046) reveals a dimeric assembly with PH-LRR on a plane flanked by the helical dimerization domain and CBR-bound CP; an 'antenna' motif connecting the helical domain to CBR-CP contacts the LRR-LRR dimer interface and mediates partial autoinhibition. Disruption of the antenna partially relieves autoinhibition in vitro and increases cell area in knockout cells; deletion of the proline-rich (myosin-I-binding) domain induces membrane spikes. Crystal structure, in vitro uncapping assay, CARMIL1 knockout rescue with mutants, cell area imaging Science advances High 41861019
2026 The membrane-binding (MB) domain of CARMIL targets the CPI and CSI motifs to lipid membranes (lipid-coated beads), enabling activation of CP for Arp2/3-mediated actin assembly; upon CP binding, the MB domain can dissociate from the membrane, enhancing uncapping of capped barbed ends and further activating soluble CP beyond what is seen in the membrane-attached state. In vitro reconstitution with lipid-coated beads, pyrene-actin polymerization assay, domain deletion mutants The Journal of biological chemistry High 42031174

Source papers

Stage 0 corpus · 35 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. The Journal of cell biology 146 11425877
2005 Mammalian CARMIL inhibits actin filament capping by capping protein. Developmental cell 109 16054028
2014 Capping protein regulatory cycle driven by CARMIL and V-1 may promote actin network assembly at protruding edges. Proceedings of the National Academy of Sciences of the United States of America 61 24778263
2009 Distinct roles for CARMIL isoforms in cell migration. Molecular biology of the cell 61 19846667
2009 An experimentally based computer search identifies unstructured membrane-binding sites in proteins: application to class I myosins, PAKS, and CARMIL. The Journal of biological chemistry 59 20018884
2006 CARMIL is a potent capping protein antagonist: identification of a conserved CARMIL domain that inhibits the activity of capping protein and uncaps capped actin filaments. The Journal of biological chemistry 54 16434392
2009 Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3. The Journal of biological chemistry 52 19926785
2015 Platelet count mediates the contribution of a genetic variant in LRRC16A to ARDS risk. Chest 40 25254322
2017 CARMIL family proteins as multidomain regulators of actin-based motility. Molecular biology of the cell 39 28663287
2017 A Missense Genetic Variant in LRRC16A/CARMIL1 Improves Acute Respiratory Distress Syndrome Survival by Attenuating Platelet Count Decline. American journal of respiratory and critical care medicine 35 27768389
2013 CARMIL leading edge localization depends on a non-canonical PH domain and dimerization. Nature communications 34 24071777
2013 Common variant of leucine-rich repeat-containing 16A (LRRC16A) gene is associated with gout susceptibility. Human cell 33 24318514
2013 Physiological role of the interaction between CARMIL1 and capping protein. Molecular biology of the cell 31 23904264
2012 Mechanism for CARMIL protein inhibition of heterodimeric actin-capping protein. The Journal of biological chemistry 31 22411988
2009 C. elegans CARMIL negatively regulates UNC-73/Trio function during neuronal development. Development (Cambridge, England) 31 19244282
2010 Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1. The Journal of biological chemistry 30 20630878
2003 CARMIL is a bona fide capping protein interactant. The Journal of biological chemistry 28 14594951
2018 Allosteric Coupling of CARMIL and V-1 Binding to Capping Protein Revealed by Hydrogen-Deuterium Exchange. Cell reports 21 29847807
2020 The Leucine-Rich Repeat Region of CARMIL1 Regulates IL-1-Mediated ERK Activation, MMP Expression, and Collagen Degradation. Cell reports 17 32610117
2011 Actin capping protein and its inhibitor CARMIL: how intrinsically disordered regions function. Physical biology 14 21572169
2025 Phosphoproteomic Analysis of CARMIL1 Reveals Novel Regulatory Mechanisms and Upstream Kinases Involved in Actin Dynamics and Cell Migration. Cytoskeleton (Hoboken, N.J.) 10 40521964
2024 CARMIL1 regulates liver cancer cell proliferation by activating the ERK/mTOR pathway through the TRIM27/p53 axis. International immunopharmacology 8 38739978
2024 CARMIL1-AA selectively inhibits macropinocytosis while sparing autophagy. Molecular biology of the cell 5 39602282
2022 Dual regulation of the actin cytoskeleton by CARMIL-GAP. Journal of cell science 5 35583107
2024 Reconstitution of Arp2/3-nucleated actin assembly with proteins CP, V-1, and CARMIL. Current biology : CB 4 39437783
2015 Differential expression of CARMIL-family genes during zebrafish development. Cytoskeleton (Hoboken, N.J.) 4 26426389
2009 Purification of capping protein using the capping protein binding site of CARMIL as an affinity matrix. Protein expression and purification 4 19427903
2023 Elastic network model reveals distinct flexibilities of capping proteins bound to CARMIL and twinfilin-tail. Proteins 3 37497763
2025 Coordinated regulation of Capping Protein by CARMIL and V-1/myotrophin. The Journal of biological chemistry 1 41354342
2021 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) 1 34150204
2026 Biochemical Functions of the Membrane-Binding Domain of CARMIL. bioRxiv : the preprint server for biology 0 41542519
2026 Linc-ROR orchestrates autophagy suppression and marks gastric cancer via the miR-145-5p/CARMIL1 axis. Cell biology and toxicology 0 41688632
2026 Mechanisms of CARMIL dimerization, autoinhibition, and capping protein binding. Science advances 0 41861019
2026 CARMIL Membrane-Binding Domain Regulates Capping Protein and Actin Assembly. The Journal of biological chemistry 0 42031174
2024 Reconstitution of Arp2/3-Nucleated Actin Assembly with CP, V-1 and CARMIL. bioRxiv : the preprint server for biology 0 38798690