CARMIL2 is a multidomain cytoskeletal regulator and signaling adaptor. It binds the actin-capping-protein heterodimer and modulates barbed-end capping, helping organize peripheral actin networks. Distinct regions support peripheral membrane association and localization along vimentin intermediate filaments. In human cultured cells, these activities contribute to polarized protrusions, collective migration and invadopodia. Signaling-competent splice forms in lymphocytes also organize CD28-dependent signaling to CARD11 and NF-kappaB through a function separable from capping-protein binding. The predominant leukocyte splice form differs from the longest reported product. Biallelic loss of CARMIL2 causes combined immunodeficiency with defects extending beyond CD28 responses.
Definition: Binding to an actin filament capping protein or capping-protein complex and directly decreasing its ability to cap actin filament ends, without covalently modifying the target.
Justification: Human CARMIL2 binds the CP heterodimer and reduces its capping activity in purified reconstitution; CBR added after capping promotes uncapping, and CPI-motif mutation loses both effects. Protein-containing complex binding omits this regulatory output. Molecular function inhibitor activity is an applicable existing parent but lacks CP specificity. The proposed activity belongs to the regulator, not to the CP target and not to a motor or enzyme by implication. GO:2000813 already records the associated biological process; no redundant NEW capping-process annotation is proposed.
Parent term: molecular function inhibitor activity
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001726 ruffle | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 localizes to membrane ruffles in migrating human cells. Reason: Live and fixed-cell imaging in human HT1080 cells places CARMIL2 at leading-edge ruffles. This localization is consistent with its local capping-protein regulatory activity; it is not inferred solely from a migration defect. Supporting Evidence: |
| GO:0001726 ruffle | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 is present at actin-rich membrane ruffles. Reason: The membrane-domain study imaged human CARMIL2b at ruffles together with actin-network markers. The selected primary Results distinguish these ruffles from the macropinosomes that subsequently form. Supporting Evidence: |
| GO:0001726 ruffle | IEA GO_REF:0000044 | ACCEPT | Summary: The mapped ruffle location is experimentally supported. Reason: The UniProt subcellular-location mapping agrees with direct human CARMIL2 imaging in PMID:26466680 and PMID:26578515. This is a localization claim, not an inference that CARMIL2 alone builds the ruffle. |
| GO:0005543 phospholipid binding | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: A basic and hydrophobic CARMIL2 segment binds membrane lipids directly. Reason: PMID:26578515 tested a purified GST fusion containing the 27-residue membrane-binding segment with brain-lipid liposomes, including GST and no-lipid controls. Together with loss of membrane targeting after mutation, this supports broad phospholipid binding. The experiment does not identify a unique phospholipid headgroup or assign this activity to the PH domain. Supporting Evidence: PMID:26578515 purified protein to lipids |
| GO:0005737 cytoplasm | IDA PMID:19846667 Distinct roles for CARMIL isoforms in cell migration. | ACCEPT | Summary: CARMIL2 is an intracellular cytoplasmic protein. Reason: The 2009 human HT1080 study visualized CARMIL2 in the cytoplasm, notably along vimentin intermediate filaments. This location is compatible with its additional peripheral membrane pool. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: Cytoplasmic CARMIL2 associates with dynamic vimentin filaments. Reason: The human-cell imaging and domain-swap experiments in PMID:26466680 establish a cytoplasmic intermediate-filament-associated pool. They do not imply that every cytoplasmic CARMIL2 molecule is filament-bound. Supporting Evidence: |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: The automated cytoplasm assignment agrees with direct localization. Reason: Independent human-cell imaging in PMID:19846667 and PMID:26466680 supports cytoplasmic localization. The broad location can therefore be retained without assuming that the uninspected ARBA rule establishes a separate mechanism. |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | ACCEPT | Summary: CARMIL2 localizes to cytoskeletal structures. Reason: Human imaging supports association with vimentin intermediate filaments and peripheral actin-rich structures. The broad UniProt location mapping is sound, although the more specific source annotations describe the relevant structures more precisely. |
| GO:0005886 plasma membrane | EXP PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 localizes at the cell periphery and plasma membrane. Reason: PMID:26466680 identifies peripheral CARMIL2 associated with leading-edge protrusions, and the independent membrane-domain study directly tests membrane targeting. This is a peripheral association rather than evidence of an integral membrane protein. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: CARMIL2 acts at the plasma membrane during cortical actin organization. Reason: Direct human membrane localization and functional rescue with membrane-targeting mutants support the location and activity asserted by the IBA. The target accession in WITH/FROM is legitimate descendant evidence, not circular support. The precise PAINT ancestral placement was not independently reconstructed, and no loss of this membrane function is indicated. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: A short CARMIL2 membrane-binding segment targets the plasma membrane. Reason: Human CARMIL2b constructs and lipid-binding assays in PMID:26578515 map peripheral membrane association to a basic and hydrophobic C-terminal segment. Membrane-binding mutants lose the peripheral pool while retaining intermediate-filament localization. Supporting Evidence: |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: The automated plasma-membrane location has direct experimental support. Reason: The combined ARBA and UniProt subcellular-location mapping agrees with the human membrane-targeting and imaging experiments in PMID:26578515. It does not imply a transmembrane topology. Supporting Evidence: |
| GO:0007163 establishment or maintenance of cell polarity | IDA PMID:19846667 Distinct roles for CARMIL isoforms in cell migration. | ACCEPT | Summary: CARMIL2 helps establish the polarized organization of migrating cells. Reason: In human HT1080 cells, depletion disrupts the unipolar cell shape and orientation of the Golgi and microtubule-organizing center. These experiments support a cell-polarity role linked to cytoskeletal organization, without generalizing to tissue-axis specification. Supporting Evidence: |
| GO:0010592 positive regulation of lamellipodium assembly | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 promotes assembly of leading-edge lamellipodia. Reason: Human CARMIL2 depletion reduces lamellipodial actin and capping-protein accumulation, and wild-type rescue restores these structures. Failure of the CP-binding mutant to rescue connects the phenotype to CARMIL2 regulation of the actin-capping machinery rather than to necessity evidence alone. Supporting Evidence: |
| GO:0015629 actin cytoskeleton | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 localizes to cortical actin structures. Reason: The 2016 membrane-domain study shows human CARMIL2 at lamellipodia and ruffles with F-actin and associated regulators. Colocalization supports membership in this cellular structure; it does not establish direct binding to actin filaments. Supporting Evidence: |
| GO:0015629 actin cytoskeleton | IEA GO_REF:0000117 | ACCEPT | Summary: The automated actin-cytoskeleton location agrees with microscopy. Reason: The direct human-cell localization in PMID:26578515 supports this broad cellular-component assignment. This decision does not reinterpret the automated rule as evidence of direct actin binding. Supporting Evidence: |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Membrane association is documented for this protein, so the generic membrane term is true, but it is not the protein's core location. Reason: Plasma membrane by EXP and IDA leads; CARMIL2 is a membrane-cytoskeleton linker (UniProt function). Membrane is true; generic. (Manual re-review for OMICS_EVIDENCE, 2026-10-10; previous action: UNDECIDED.) Supporting Evidence: |
| GO:0016477 cell migration | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: CARMIL2 supports collective cell migration in a context-dependent manner. Reason: Direct human experiments support collective migration into a scratch gap, while random single-cell migration was unaffected in the 2015 HT1080 conditions. The inherited process is plausible and the human accession in WITH/FROM is valid descendant evidence. Migration is retained as an outcome of cytoskeletal organization rather than a separate molecular core; this is not a challenge based on donor count. |
| GO:0030027 lamellipodium | IBA GO_REF:0000033 | ACCEPT | Summary: CARMIL2 is active in lamellipodial actin organization. Reason: Human localization and membrane-mutant rescue experiments support a functional lamellipodial pool. These target data agree with the inherited location without requiring a new reconstruction of the PAINT node. Inclusion of the target among the descendant sources is appropriate. |
| GO:0030027 lamellipodium | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 is present at lamellipodia. Reason: Human CARMIL2b colocalizes with actin-network markers at lamellipodia in PMID:26578515. The membrane-binding segment is important for this peripheral localization. Supporting Evidence: |
| GO:0030027 lamellipodium | IEA GO_REF:0000044 | ACCEPT | Summary: The mapped lamellipodium location is directly supported. Reason: The UniProt subcellular-location mapping agrees with the human microscopy in PMID:26578515 and the leading-edge functional analysis in PMID:26466680. Supporting Evidence: |
| GO:0030335 positive regulation of cell migration | IDA PMID:19846667 Distinct roles for CARMIL isoforms in cell migration. | KEEP AS NON CORE | Summary: CARMIL2 promotes migration of a human cell monolayer into a gap. Reason: The 2009 HT1080 depletion experiments reduced scratch-wound migration and disrupted polarized cell organization. This is a supported cellular consequence of CARMIL2 function, retained as non-core rather than generalized to every migration mode. Supporting Evidence: |
| GO:0030335 positive regulation of cell migration | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | KEEP AS NON CORE | Summary: CARMIL2 supports directional collective migration. Reason: The 2015 scratch assay showed impaired collective migration after depletion, but random single-cell movement was not reduced. A CP-binding-deficient CARMIL2 mutant rescued collective migration even though it failed to rescue several protrusion phenotypes. Thus this migration role must not be described as obligatorily CP-binding-dependent. Supporting Evidence: |
| GO:0030335 positive regulation of cell migration | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | KEEP AS NON CORE | Summary: CARMIL2 membrane targeting contributes to collective migration. Reason: The 2016 membrane-binding mutants failed to rescue scratch-gap migration in human HT1080 cells. This supports the positive regulatory process in that setting, not a universal increase in motility or a direct motor activity. Supporting Evidence: |
| GO:0031234 extrinsic component of cytoplasmic side of plasma membrane | NAS PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 is a peripheral protein on the cytoplasmic face of the plasma membrane. Reason: CARMIL2 is an intracellular cytoskeletal regulator whose basic and hydrophobic segment binds lipids and targets the cell periphery. The human membrane-domain experiments support the stated peripheral topology; no membrane-spanning or extracellular localization is implied. Supporting Evidence: |
| GO:0031252 cell leading edge | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 localizes to the leading edge of migrating cells. Reason: PMID:26466680 imaged CARMIL2 at peripheral actin-rich protrusions and on dynamic vimentin filaments directed toward the leading edge. The location is supported directly in human HT1080 cells. Supporting Evidence: |
| GO:0034315 regulation of Arp2/3 complex-mediated actin nucleation | IBA GO_REF:0000033 | UNDECIDED | Summary: The precise inherited Arp2/3-nucleation regulatory claim remains unresolved. Reason: The IBA represents an ancestral PAINT judgment, not a pairwise transfer, and its single listed Dictyostelium descendant is not intrinsically weak evidence. Human CARMIL2 directly regulates capping protein and cortical actin networks, which is compatible with indirect regulation of Arp2/3-dependent assembly. However, the actual IBD placement and the donor experiment underlying this specific nucleation-regulation assertion were not inspected. Neither absence of demonstrated direct Arp2/3 binding nor capping regulation alone settles this process assignment. Supporting Evidence: |
| GO:0044319 wound healing, spreading of cells | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | KEEP AS NON CORE | Summary: CARMIL2 contributes to collective cell movement across a scratch gap. Reason: The official GO definition of wound healing, spreading of cells includes cell migration across the wound gap to restore a continuous surface. The human scratch assay therefore fits this term; it need not be rejected as a mismatch between migration and spreading. Retain as a contextual cellular outcome, without claiming organismal wound repair or obligatory CP-binding dependence. Supporting Evidence: |
| GO:0044319 wound healing, spreading of cells | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | KEEP AS NON CORE | Summary: CARMIL2 membrane targeting supports cell movement across an experimental gap. Reason: The 2016 human monolayer scratch experiment and rescue analysis support this process as defined by GO, which includes migration across a wound gap. The evidence is cellular and does not independently establish a role in physiological tissue repair. Supporting Evidence: |
| GO:0044354 macropinosome | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 localizes to macropinosomes derived from membrane ruffles. Reason: Selected primary imaging in PMID:26578515 distinguishes CARMIL2-positive macropinosomal structures from leading-edge ruffles and follows their marker composition. This is a localization claim, not evidence that CARMIL2 is a vesicle enzyme. Supporting Evidence: |
| GO:0044877 protein-containing complex binding | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | MODIFY | Summary: CARMIL2 directly inhibits the actin-capping-protein complex through its CP-binding region. Reason: The original complex-binding assertion is sound, but the same primary study establishes a molecular regulatory activity beyond association. Purified human CARMIL2 CBR (the study construct residues 961–1072) relieves CP-mediated inhibition of seeded actin polymerization and promotes uncapping when added after CP; the RR985/987AA mutant loses these effects. Full-length wild-type, but not mutant, CARMIL2 coprecipitates CP from HT1080 cells. GO:0140678 captures direct noncovalent inhibition of a target activity without implying that CP is an enzyme or that CARMIL2 itself caps actin. A proposed CP-specific child term records the remaining ontology specificity gap. The biochemical result is from the isolated CBR, not a claim that every whole-protein cellular role is inhibitory or CP-dependent. Proposed replacements: molecular function inhibitor activity Supporting Evidence: |
| GO:0045111 intermediate filament cytoskeleton | IDA PMID:19846667 Distinct roles for CARMIL isoforms in cell migration. | ACCEPT | Summary: CARMIL2 associates with the vimentin intermediate-filament cytoskeleton. Reason: Human HT1080 imaging in the 2009 primary study shows CARMIL2 along vimentin rather than keratin filaments. This cellular-component annotation does not require or establish purified binary binding to vimentin. Supporting Evidence: |
| GO:0045111 intermediate filament cytoskeleton | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: The CARMIL2 LRR region targets dynamic vimentin filaments. Reason: Human-cell imaging and CARMIL1/CARMIL2 domain swaps in PMID:26466680 support an LRR-dependent intermediate-filament-associated pool. The experiments establish localization and functional coupling, not a purified direct CARMIL2-vimentin interaction. Supporting Evidence: |
| GO:0045111 intermediate filament cytoskeleton | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 retains intermediate-filament localization independently of its membrane-binding segment. Reason: In the membrane-domain study, wild-type CARMIL2 and membrane-binding-deficient variants retain filament-associated localization. This supports an intermediate-filament pool distinct from the peripheral actin-associated pool. Supporting Evidence: |
| GO:0051639 actin filament network formation | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 contributes to formation of cortical actin networks through CP regulation. Reason: In human cells, depletion and rescue experiments connect CARMIL2 to lamellipodial and ruffle actin assembly. The CP-binding mutant separates this role from CP-independent collective migration, and purified CARMIL2-CP assays identify a molecular step performed by CARMIL2. Supporting Evidence: |
| GO:0051639 actin filament network formation | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: Membrane-associated CARMIL2 supports assembly of peripheral actin networks. Reason: The human membrane-domain mutants retain filament localization but fail to restore normal leading-edge actin and CP organization. The interpretation is supported by direct membrane binding and the independently demonstrated CP-regulatory activity, rather than by an unexplained depletion phenotype alone. Supporting Evidence: |
| GO:0061339 establishment or maintenance of monopolar cell polarity | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 helps maintain a single polarized leading-edge organization. Reason: The primary human-cell shape and rescue analysis distinguishes unipolar from multipolar or apolar organization. This matches the GO definition of monopolar cell polarity; it does not imply an organism-specific developmental polarity mechanism. Supporting Evidence: |
| GO:0061339 establishment or maintenance of monopolar cell polarity | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 membrane binding is important for unipolar cell organization. Reason: The 2016 membrane-binding mutants failed to rescue the polarized human HT1080 cell morphology. This supports establishment or maintenance of a single cellular polarity axis in the studied migration context. Supporting Evidence: |
| GO:0090091 positive regulation of extracellular matrix disassembly | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | KEEP AS NON CORE | Summary: CARMIL2 supports invadopodial matrix degradation through actin organization. Reason: Human HT1080 depletion and rescue experiments measured invadopodial actin structures and gelatin degradation. CP-binding and intermediate-filament targeting were required for this phenotype. The positive regulatory process is supported in this tumor-cell context; CARMIL2 is not assigned extracellular protease activity. Supporting Evidence: |
| GO:0090091 positive regulation of extracellular matrix disassembly | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | KEEP AS NON CORE | Summary: CARMIL2 membrane binding contributes to invadopodia-dependent matrix degradation. Reason: The membrane-domain study measured gelatin degradation and invadopodial structures in human cells, with loss of rescue by membrane-binding mutants. This is a context-dependent consequence of the cortical organizer function rather than direct matrix cleavage by CARMIL2. Supporting Evidence: |
| GO:0160108 animal gross anatomical part developmental process | IEA GO_REF:0000117 | UNDECIDED | Summary: The broad automated gross-anatomical-development assignment is not resolved. Reason: The ARBA rule and its underlying training evidence were not inspected. The reviewed studies establish cytoskeletal organization and immune-cell signaling or differentiation, but those facts alone do not establish participation in development of an animal gross anatomical part. Retain uncertainty rather than converting a broad automated assertion into a confident developmental function or treating lack of a reviewed developmental experiment as proof of error. |
| GO:1900029 positive regulation of ruffle assembly | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 promotes membrane-ruffle assembly through its actin-regulatory function. Reason: The human depletion/rescue experiments in PMID:26466680 connect ruffle formation to both CP binding and appropriate localization. Direct CP-regulatory activity supplies a mechanistic contribution to the assembly process. Supporting Evidence: |
| GO:1900029 positive regulation of ruffle assembly | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 membrane targeting promotes ruffle assembly. Reason: Human CARMIL2 membrane-binding mutants fail to restore normal ruffling despite retaining intermediate-filament localization. The phenotype is consistent with local control of actin-capping machinery at the cell edge. Supporting Evidence: |
| GO:1902745 positive regulation of lamellipodium organization | IDA PMID:26578515 Cell Migration and Invadopodia Formation Require a Membrane-... | ACCEPT | Summary: CARMIL2 membrane binding supports organized lamellipodia. Reason: The 2016 human-cell rescue experiments link membrane targeting to proper peripheral actin and CP organization. The annotation describes organization of the lamellipodium rather than direct actin nucleation by CARMIL2. Supporting Evidence: |
| GO:2000813 negative regulation of barbed-end actin filament capping | IDA PMID:26466680 CARMIL2 is a novel molecular connection between vimentin and... | ACCEPT | Summary: CARMIL2 decreases CP-mediated barbed-end capping and promotes uncapping. Reason: Purified CARMIL2 CBR was tested with capping protein and actin in polymerization assays in PMID:26466680. The experiments show reduced capping and uncapping of previously capped filaments. The activity modulates CP rather than abolishing all CP function, and its cellular consequences depend on localization and context. Supporting Evidence: PMID:26466680 CARMIL2 binds and inhibits CP |
| GO:0035591 signaling adaptor activity | IMP PMID:27647348 The scaffolding function of the RLTPR protein explains its e... | NEW | Summary: Signaling-competent CARMIL2 splice forms organize noncatalytic CD28-to-CARD11/NF-kappaB coupling. Reason: This molecular-function proposal makes the immune-adaptor activity already represented in the core synthesis explicit. Endogenous human Jurkat PH-domain and proline-rich-region deletions disrupt co-stimulation while preserving CP association; the CPI motif is dispensable in the tested immune response. Mouse thymocyte AP-MS and recruitment experiments provide the physical-assembly context, whereas human patient and splice-form complementation studies establish functional conservation. The human isoforms called 2 and 3 in PMID:36515678 restore CD28-induced NF-kappaB responses; the longest isoform 1 does not in that assay. CARMIL2 therefore contributes scaffold activity rather than merely being a disease-associated requirement or a signaling substrate. The conclusion does not require a purified simultaneous CD28–CARMIL2–CARD11 bridge, direct binding of every partner, CBM-complex membership, or activity of every splice form. No unverified UniProt isoform identifier is assigned. This activity is distinct from the source phospholipid-binding and CP-complex-binding annotations and their CP-inhibitor refinement. |
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Download this section (compressed HTML)Q: Which PAINT ancestral evidence supports the inherited Arp2/3-nucleation regulatory activity in the CARMIL2 clade, and how does it relate to direct capping-protein regulation?
Q: Which molecular interactions mediate the CP-independent contribution of CARMIL2 to collective migration, and is its association with vimentin direct?
Q: How do the reported 1399-residue leukocyte form and the signaling-competent 1372-residue form map to current authoritative transcript and protein records, and which splice forms support cytoskeletal versus immune functions in endogenous human cells?
Q: Which CARMIL2 peptides and accession were identified in the original NK-cell membrane-proteomics table, and what evidence underlies the broad developmental ARBA rule?
Q: Which receptor- and cell-context-specific process annotations should accompany the demonstrated CARMIL2 signaling-adaptor activity, after comparing other intracellular costimulatory adaptors and resolving the reported splice forms against authoritative protein records?
Experiment: Compare endogenous CARMIL2 rescue with matched CP-binding-deficient and membrane-targeting-deficient variants in human immune and migratory cells, measuring local actin organization and CD28-to-CARD11/NF-kappaB signaling separately.
Experiment: Reconstitute the candidate CARMIL2-vimentin interaction with purified components while testing whether it changes delivery or regulation of the actin-capping-protein heterodimer.
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