Human CORO1A encodes coronin-1A, a 461-residue WD-repeat protein with a C-terminal coiled-coil region. The official record lists no alternative products. Actin binding, cortical organization and immune-cell behavior form its best-established integrated activity, but the proportion of protein associated with actin varies with cell type, activation state and measurement method. PMID:15601263(https://pubmed.ncbi.nlm.nih.gov/15601263/), PMID:24760828(https://pubmed.ncbi.nlm.nih.gov/24760828/), PMID:42611950(https://pubmed.ncbi.nlm.nih.gov/42611950/).
The human self-association study uses recombinant protein, coexpression and leucine-zipper mutants. Its hydrodynamic measurements were interpreted as a dimer, whereas the later mouse J774/native-protein and synthetic 430–461 peptide study supports a trimeric coiled coil and questions the earlier sizing interpretation. Both support homotypic association. GO:0042802 preserves that shared result without asserting a settled native human oligomer distribution. The different constructs and species are not interchangeable. PMID:15601263(https://doi.org/10.1042/BJ20041020), PMID:15800061(https://pubmed.ncbi.nlm.nih.gov/15800061/).
Human full-length GST-CORO1A inhibits Arp2/3/VCA-dependent pyrene-actin nucleation; GST and the isolated WD region do not reproduce this activity. This supports GO:0034316 rather than an unspecified effect on all actin polymerization. Dominant-negative cell phenotypes in the same paper may involve several coronins. The primary assay and its short literal passage are identified in the source excerpts. PMID:17442961(https://doi.org/10.4049/jimmunol.178.9.5769).
The phosphorylation paper tests both intact protein and a separate EGFP-p57LZ fragment spanning residues 372–461. Added G-actin binds the immunopurified fragment, with T412 substitutions affecting this assay. Full-length wild-type and mutant F-actin co-sedimentation is similar. Therefore phosphorylation-sensitive fragment binding does not establish suppression of all intact-protein F-actin binding. The available cached text omits Methods and Results; the original PMC Methods and Results resolve this distinction. PMID:23100250(https://pmc.ncbi.nlm.nih.gov/articles/PMC3522287/).
Human NK-cell knockdown and patient cells show altered synaptic F-actin density and impaired access of lytic granules. They retain the ability to form a synapse, so the existing NOT-synapse-formation annotation is compatible with positive synaptic localization and meshwork remodeling. No purified actin-severing activity is inferred. The study emphasizing CORO1C also directly assays human CORO1A wild-type/R29D binding, which is retained without transferring CORO1C-specific cooperativity. PMID:24760828(https://pmc.ncbi.nlm.nih.gov/articles/PMC4020046/), PMID:22364218(https://pubmed.ncbi.nlm.nih.gov/22364218/).
The 2026 native-protein study qualifies broad localization claims. Bulk endogenous coronins can behave independently of F-actin in the tested conditions. GFP increases imaging colocalization but does not demonstrate increased actin-dependent pelleting. Its CORO1B/C repolymerization and cAMP experiments are not CORO1A experiments. These findings limit generalization while leaving the earlier direct biochemical and human NK-cell evidence intact. PMID:42611950(https://pubmed.ncbi.nlm.nih.gov/42611950/).
In differentiated human HL60 cells, PKC inhibitors retain p57 and F-actin on phagosomes and reduce LAMP1 recruitment. Purified p57 is a PKC substrate, but the original discussion explicitly allows other substrates, including MARCKS and pleckstrin, to explain the inhibitor effect. The phagosome–lysosome fusion assertion is therefore over-annotated for this source; positive localization and phosphorylation are preserved. A selective CORO1A perturbation with fusion measurements would distinguish its contribution from parallel PKC substrates. The full original is available at J-STAGE, pages 837–844; see the Discussion excerpt. PMID:12132654(https://pubmed.ncbi.nlm.nih.gov/12132654/).
The original PI3K paper reports a negative anti-p85 co-precipitation result in Results 3.1. Its positive observations concern regulated coronin pools, phox association and early-phagosome colocalization. These do not establish physical PI3K binding. Removal is confined to that positive binding assertion and citation; it is not a universal absence claim. The later PI3Kδ survival study was accessible only as an abstract and institutional metadata, so its full interaction experiments remain unassessed. PMID:11094157(https://doi.org/10.1016/S0014-5793(00)02220-1), PMID:34932374(https://doi.org/10.1126/scisignal.abj0057).
Native human neutrophil and recombinant experiments support p40phox/NCF4 interaction and association with phox complexes. The bacterial LpdC study supports cholesterol-dependent capture and a non-core enzyme-binding refinement. Its cellular experiments use mouse J774 cells; the recovered GST-coronin Methods do not explicitly identify the coronin species. Human Reactome mapping and the original curator assertion are preserved with that reagent limit. NCF1 and NCF4 are noncatalytic oxidase-complex subunits, not evidence that CORO1A catalyzes oxidase activity. PMID:9365277(https://pubmed.ncbi.nlm.nih.gov/9365277/), PMID:17652161(https://pubmed.ncbi.nlm.nih.gov/17652161/), Reactome R-HSA-9636396.
Human-cell/tissue staining supports cytoplasmic and peripheral localization; the source explicitly excludes nuclear staining in HL60 cells and rat microglia. That source-specific negation does not imply universal nuclear absence. Mouse endosome, axonal and synaptic annotations remain ortholog-scoped and non-core. The Rltpr-focused junction paper was not fully recovered for the precise CORO1A panel; its title alone cannot refute the curator's target annotation. PMID:17341475(https://doi.org/10.1369/jhc.6A7156.2007), PMID:24270184(https://pubmed.ncbi.nlm.nih.gov/24270184/), PMID:24667537(https://pubmed.ncbi.nlm.nih.gov/24667537/).
The exact interaction records and product checks support partner-specific refinements: STAT3 to STAT-family binding, GM130 to cytoskeletal-regulatory protein binding, and MAGEA11 to transcription-coactivator binding. These describe the partner class and do not assign those partners' functions to CORO1A. The MAGEA11 screen specifies residues 111–429; the independent activity literature tests the corresponding 112–429 androgen-receptor-interacting form. FSD2, IFT20-3 and APP interactions remain positive non-core observations because a more specific activity class is not established at the tested scope. Variant features are retained rather than erased by reference-sequence matches. PMID:21988832(https://pubmed.ncbi.nlm.nih.gov/21988832/), PMID:25416956(https://pubmed.ncbi.nlm.nih.gov/25416956/), PMID:32296183(https://pubmed.ncbi.nlm.nih.gov/32296183/), PMID:32814053(https://pubmed.ncbi.nlm.nih.gov/32814053/).
The original HeLa mRNA-interactome workbook places CORO1A in Table S1 row 183, with ion-count adjusted P = 0.00245116. Its crosslinked and control identification columns both say not identified. The study explicitly distinguishes the significantly enriched ion-count subset from the separately identified protein set. UV crosslinking and stringent oligo(dT)/RNase purification support a positive RNA-contact observation, without establishing RNA regulation as a principal function. PMID:22658674(https://pubmed.ncbi.nlm.nih.gov/22658674/).
The original human RN B-cell exosome paper's Figure 2 lists CORO1A. The experiment used differential centrifugation, sucrose separation and MHCII immunoadsorption, with two unique peptides in at least two of three experiments. Its GO-category display does not independently assay leading-edge localization. The EPS-urine study's main Methods are available, but its exact CORO1A supplementary row remains unrecovered. Challenged HTML responses are not readable workbooks. Both exosome annotations remain non-core, and fluid detection does not establish a particular cell of origin. PMID:20458337(https://pubmed.ncbi.nlm.nih.gov/20458337/), PMID:23533145(https://pubmed.ncbi.nlm.nih.gov/23533145/).
Mouse E26K alters localization and Arp2/3 regulation without abolishing F-actin binding. Human severe immunodeficiency cases establish loss or marked reduction of CORO1A protein and profound T-cell defects. The patient carrying a larger deletion has many additional affected genes, so associated neurodevelopmental features cannot be uniquely assigned to CORO1A. PMID:18836449(https://pubmed.ncbi.nlm.nih.gov/18836449/), PMID:19097825(https://pubmed.ncbi.nlm.nih.gov/19097825/), PMID:23522482(https://pubmed.ncbi.nlm.nih.gov/23522482/).
The 2026 vesicle study supports human-cell CORO1A-dependent changes in extracellular-vesicle output and CD63-pHluorin fusion events, including reduced baseline release after knockout. Much mechanistic dissection uses neddylation inhibition. CORO1A coimmunoprecipitates with PKM2 rather than SNAP23; the upstream tyrosine kinase and its proposed recruitment remain unresolved. The purified lipid-fusion assay contains SNARE proteins and no CORO1A. These positive regulatory observations belong alongside the established biology, without assigning intrinsic kinase, fusogen or demonstrated dual-binding adaptor activity. They do not convert extracellular-vesicle cargo detection into a secretion mechanism. PMID:42265296(https://doi.org/10.1038/s42003-026-10424-4).
One integrated actin-binding/cortical-network core captures the supported biochemical and immune-cell work. Specialized RNA, phox, bacterial-enzyme, neuronal and vesicle observations retain their individual evidence limits. No new annotation is proposed from necessity alone or from an untested kinase-recruitment model. Current donor identities and ARBA conditions are inspectable in the source evidence index; historical PAINT node placements and Compara alignments remain unresolved rather than being inferred from donor counts.
Purified full-length human GST-CORO1A inhibits Arp2/3/VCA-dependent actin nucleation, whereas the isolated WD construct does not. The integrated actin-binding core now names this already reviewed specific process. It does not duplicate the broader ontology ancestor as a second process or assert that every NK-cell architectural phenotype operates through this mechanism. The dominant-negative cellular experiments can affect multiple coronins and remain distinct from the purified full-length assay. PMID:17442961(https://doi.org/10.4049/jimmunol.178.9.5769), Results and Figure10.
The human NK study establishes control of local actin meshwork density, area, volume and granule-permissive openings. CORO1A deficiency did not redistribute bulk G/F-actin or increase total synaptic F-actin. F-actin stabilization phenocopied aspects of the architectural defect, supporting dynamic remodeling; it did not distinguish filament depolymerization from altered branching or spatial rearrangement. The existing regulation-of-actin-cytoskeleton assertion is therefore retained. A depolymerization-regulation term does not require direct severing by CORO1A, but it still specifies increased depolymerization that these measurements do not separately resolve. The authors' positive deconstruction findings and possible local depolymerization remain intact. PMID:24760828(https://pmc.ncbi.nlm.nih.gov/articles/PMC4020046/), Results Figures2–5 and Discussion.
The phagolysosome assessment is source-specific. In differentiated human HL60 cells, the PKC inhibitor prevents p57/F-actin dissociation and reduces LAMP1 recruitment, but the original Discussion explicitly allows other phagosomal PKC substrates to explain the effect. The separate Cell2007 study reports coronin-dependent calcium/calcineurin signaling that inhibits lysosomal delivery in mycobacteria-infected mouse macrophages. Its complete abstract was read; original full text remains unavailable after bounded recovery. These different contexts support regulation of trafficking without establishing an invariant positive or negative role in all phagosome–lysosome fusion. The human PKC result is not rejected solely because a mouse infection experiment has an inhibitory direction. PMID:12132654(https://www.jstage.jst.go.jp/article/bpb/25/7/25_7_837/_pdf), Figure6 and Discussion p843; PMID:17632055(https://pubmed.ncbi.nlm.nih.gov/17632055/), complete abstract.
The anti-p85 result supporting the source-specific PI3K-binding removal can be inspected in the original publisher text, Results3.1. The phagolysosome caveat is in the original Japanese Society PDF, Discussion p843. The short excerpt page transcribes those original passages with explicit locators; it is not a separate experiment, and its automated substring check does not independently establish source authenticity. Both original passages have been read separately. Their saved source hashes and transcription checks are recorded in the source-evidence index. The normal abstract caches remain unchanged.
The human self-association experiment and the separate mouse-derived identical-protein-binding assertion remain separately represented. The human dimer-to-identical-binding refinement preserves positive experimental self-association without forcing the later mouse trimer estimate onto human CORO1A. Neither source creates a second core or a NEW assertion. PMID:15601263(https://pubmed.ncbi.nlm.nih.gov/15601263/), PMID:15800061(https://pubmed.ncbi.nlm.nih.gov/15800061/).
The peripheral T-cell PI3Kdelta survival pathway remains positive biological context. Its available abstract does not settle the molecular contact or the precise target-performed step; the corresponding biological question is now explicit. No new survival-process assertion is manufactured from necessity alone. PMID:34932374(https://pubmed.ncbi.nlm.nih.gov/34932374/).