Current synthesis: ANXA11 has calcium-dependent membrane-binding and protein–membrane adaptor activities, and a separately demonstrated structural role in the midbody matrix. The exact molecular mechanism of its cytokinesis role remains unresolved. The dated entries below preserve the research chronology; later closure and PR follow-up sections supersede historical PENDING and source-access statements.
Human ANXA11 (UniProt P50995; synonym ANX11) encodes annexin A11, a calcium-responsive phospholipid-binding protein with an extended low-complexity N-terminal region and a C-terminal annexin-repeat region. The imported seed contains 69 original annotations and two alternative products, P50995-1 and P50995-2. All original annotation objects remain PENDING while the evidence map is prepared for independent annotation consultation. The original YAML, UniProt and GOA bytes are protected in tmp/ANXA11-initial/; no seed retrieval was repeated.
The fresh main/alias/history/branch/open-PR check passed at main 7a664d7f5a2565dc65a77cc8eacccd0e9becfa90: ANXA11/ANX11 gene and history directories and the task branch were absent, and the complete 64-entry open-PR inventory contained no matching gene. This is an initial preflight, not a future publication race check.
All 22 PMID references seeded into the review already have normal cached records: eight carry full-text availability flags and 14 are abstract-only. A flag is not proof that every experiment or supplement has been read. The full source census and initial row identities are recorded in tmp/ANXA11-initial/initial-source-census.json.
The installed-client Falcon attempt with the configured Perplexity-lite fallback terminated without producing a report. Falcon authentication failed; fallback name resolution failed. The terminal receipt and a sharing-safe redacted log are under tmp/ANXA11-initial/. No manually written provider file was created. The raw provider traceback contains authentication debug locals and must remain local, not be copied into publication artifacts.
The principal working model is a calcium-controlled connection between membranes and cytoplasmic macromolecular assemblies. Nuclear/cell-cycle localization and a role in terminal cytokinesis are established in older human-cell experiments. More recent primary work directly tests ANXA11-mediated contacts between RNA granules and lysosomal membranes, rather than relying solely on a knockout phenotype. The exact GO molecular-function formulation remains to be checked; a membrane or organelle location does not by itself establish an adaptor or scaffold activity.
Five additional journal records are needed as ordinary caches. Their verified identifiers and the exact bounded read scopes are in additional-primary-assessment.json; they are not replacement caches or generated provider research.
One 45-second ordinary five-ID cache-fetch batch terminated with timeout, exit -15 and zero output files. This is one interrupted batch, not evidence of five individually completed failures. No existing publication record was overwritten; exact finite recovery is requested for these five IDs only.
The complete abstracts of the 14 abstract-only seed papers were read. Where a gene is not foregrounded, that is not evidence of a wrong-gene annotation. Full-text and pair-specific gaps remain explicit.
The IBA rows with ANXA11 itself among the descendant evidence are legitimate PAINT inheritance assertions, not circular evidence. The ancestral node placement, target membership and source experiments must be distinguished from donor counts. No PAINT-node loss, divergence or donor topology has yet been demonstrated.
Before authoring the review, finish the source-specific annotation matrix, check current GO definitions and relevant PAINT/HPA evidence, obtain independent annotation consultation, and preserve all source/alternative-product/negation identity. Any NEW process would require identifying ANXA11's own contribution, checking same-role comparators, ontology parents and cached GO-CAMs, and excluding redundant ancestors/descendants. A new process is not presumed necessary to describe the mechanistic core.
The original PMID:9268363 full article resolves the sorcin question. Methods identify human ANXA11 cDNA (IMAGE26147), a GST fusion of residues 1–121, and sequence verification. The ANXA11 Results and Figure 6 describe calcium-dependent binding of recombinant sorcin with an unfused-GST control. This supports refining the generic binding row to calcium-dependent protein binding. The separate synexin granule-aggregation experiments remain ANXA7 experiments. Only targeted ANXA11 Methods, Results, legend and relevant Discussion were inspected; the canonical abstract-only cache is unchanged.
Further PMID:15197175 Results establish controlled CHO1 co-IP specifically during late mitosis/cytokinesis, but explicitly allow a direct or indirect interaction. Tubulin also appears in the control immunoprecipitate. Therefore neither direct tubulin binding nor a demonstrated kinesin adaptor mechanism follows. Targeted PMID:28469040 Results include diffuse cytoplasmic and nuclear wild-type controls, distinct from disease-mutant inclusions, and partner-binding assays; mutant pathology is not used to define a normal core process.
The 2025 publisher Methods now resolve the construct concern: ANXA11 full length 1–505, LCD 1–185 and annexin region 186–505 were PCR-cloned from HeLa cDNA, expressed in bacteria and purified with tag cleavage. This is human sequence evidence. The earlier 1–502 wording in Results is not used to change product identity or seed residue numbering. Indexed original 2019 cloning/experimental-model Methods were also read; the study mixes human iPSC-derived neurons and rat experiments, so each assay still requires its own construct/host distinction.
Current HPA reports supported nucleoplasm and cytosol with antibody HPA027545, plus an approved vesicular pool. The live table lists nucleoplasm/cytosol in A-431, U-251MG, U2OS and RPTEC/TERT1, and nucleoplasm/vesicles in serum-starved hTERT-RPE1. Image pixels were not independently scored.
The local PTHR10502 member table contains human P50995 and mouse P97384 in PTHR10502:SF29, official label ANNEXIN A11. No local PAINT ancestral-annotation slice or complete family tree is present, so membership is verified but IBD placements are not. The GO-CAM index search for P50995/ANXA11/ANX11 found no target record.
Official GO definitions were checked for protein-macromolecule adaptor activity, protein complex scaffold activity, kinesin binding and calcium-dependent protein binding. The first permits coordinated protein–lipid/nucleic-acid contacts; the scaffold term specifically denotes an integral structural complex component. A single adaptor candidate is being considered for the experimentally reconstituted RNA-granule/membrane contact. No NEW biological process is proposed.
The prospective 69-row map is tmp/ANXA11-initial/prospective-all69-review.json: 38 ACCEPT, 5 MODIFY, 12 KEEP_AS_NON_CORE and 14 UNDECIDED before independent consultation. It explicitly flags the phagocytosis IEP/IBA confidence, the direct-or-indirect KIF23 association, cross-paper PDCD6 refinement, specialized proteomic locations and the single adaptor candidate for challenge. These are proposals only; canonical decisions remain PENDING.
The all-69-row independent annotation consultation is recorded in tmp/ANXA11-initial/alx3-independent-prospective-consultation.json. I adopt its eight uncertainty amendments: the two phagocytosis rows require process evidence beyond recruitment; the two ECM, one melanosome and three exosome rows lack inspected ANXA11-specific proteomic entries. This preserves the curated assertions without claiming that they are false. The resulting original-row proposal is 38 ACCEPT, five MODIFY, four KEEP_AS_NON_CORE and 22 UNDECIDED. Canonical review authoring follows this consultation; source closure is still pending.
The narrower molecular function GO:0043495 protein-membrane adaptor activity fits recruitment of a protein-containing RNP granule to membrane lipids. I independently read its official definition, parent GO:0030674 and children; only the narrower term is proposed. No biological-process NEW is proposed.
The original study-linked Addgene plasmid 164210 identifies the pLEX-EF1a ANXA11-mEmerald insert as human, 1515 bp, with a C-terminal fluorescent tag, and links PMID:31539493. This resolves the sequence species for that deposited imaging construct; it does not by itself establish the provenance of every purified reagent or the species of neuronal hosts.
Additional actual publisher reading of PMID:40118863 covered Results on phase coupling and granule recruitment (Figures 3–6), GUV/SUV preparation and the cell-free granule-binding Methods. Human U2OS stress granules were sorted after arsenite treatment. Full-length human ANXA11 recruited granules to mixed-lipid GUVs; naked and ARD-coated GUV controls did not. The mixture contained PS and PE, but mixture binding does not establish independent specificity for either lipid. ALG2/CALC modulated recruitment. Cellular lysosome experiments used transient expression and hypotonic swelling, so their lipid-order comparison is condition-specific. These targeted text/legend reads did not include independent inspection of figure pixels or supplementary peptide tables. Original paper.
All 69 original rows are now reviewed after the independent consultation; source fields and both alternative products are unchanged. The draft passes just validate human ANXA11. Two advisories are intentional: the directly observed but potentially indirect CHO1 association remains non-core rather than being promoted to a specific binary interface, and the calcium-dependent binding decisions distinguish resolved ALG-2 evidence from the unresolved PEF1 assertion. The single new membrane-adaptor annotation and its direct evidence attachments will be added after Source35 normal-source closure. No source cache or raw seed was changed.
All five requested ordinary records were recovered and assessed from the exact Source35 archive before parent import. The canonical copies now match the archive and each raw normal-output copy byte for byte. PMID:31539493, PMID:40118863 and PMID:42574611 carry XML full-text flags; PMID:25540196 and PMID:42364743 remain abstract-only. The flag records availability, not inspection of every experiment. The immutable initial assessment preserves its earlier scope; tmp/ANXA11-initial/source35-actual-source-assessment.json records the expanded actual-text read.
The strongest direct human membrane-adaptor experiment is PMID:40118863(https://www.nature.com/articles/s41467-025-58142-5). Actual construct Methods explicitly use HeLa cDNA for full-length 1–505, LCD 1–185 and ARD 186–505; the inconsistent 1–502 Results numbering is not used to rewrite the human products. Results/Figure 6 show that full-length ANXA11-coated GUVs recruit FAPS-isolated U2OS RNP granules. Naked GUVs, ARD-coated GUVs and purified G3BP1 alone do not recapitulate that coupling. Actual purification, construct, targeted phase/lipid and granule-binding Methods were read, with corresponding Results and legends. This supports the single NEW GO:0043495 protein-membrane adaptor activity, distinct from the existing calcium-dependent phospholipid-binding activity. No additional process or generic adaptor ancestor is proposed. ALG2/CALC regulation and model-membrane mechanics were read; hypothetical resistance to axonal shear is not treated as a measured neuronal mechanism.
Actual PMID:31539493(https://pmc.ncbi.nlm.nih.gov/articles/PMC6890474/) Results/Figure 2/Figure 6 and targeted construct, purification, droplet, granule-reconstitution and liposome Methods were read. Isolated SH-SY5Y stress-granule cores associate with phosphoinositide-containing liposomes only with ANXA11 and calcium. The Figure 6/Results formulation names PI3P, while the generic liposome-preparation recipe names PI(3,5)P2; these are recorded as source-local descriptions rather than silently fused into one recipe. Human P50995 modeling and the verified human deposited imaging construct do not prove the species of every purified reagent or rat neuronal host. The review therefore anchors direct-human NEW evidence to the HeLa-derived 2025 construct. Not every structural/neuronal method, supplementary table or image pixel was inspected.
Actual PMID:42574611(https://pmc.ncbi.nlm.nih.gov/articles/PMC13486606/) Results/Figures 6–8, Discussion and targeted cell culture, knockdown, imaging, recruitment, co-IP, purification and liposome-flotation Methods were read. The later Figure 8 is additional direct evidence: purified sorcin alone does not float with liposomes, whereas ANXA11, unlike the ANXA2 control, recruits it in calcium. The inspected Methods identify purchased Bio-Techne His6-ANXA11 without a catalogue/species, so this reagent is not automatically labelled human. Separate endogenous HCT116 co-IP and U2OS injury experiments establish the human-cell context. The paper includes one Discussion sentence reversing the sorcin-domain assignment stated in its Abstract/Results; the review avoids that isolated reversal and does not need a detailed domain claim. Viral-budding and calpain suggestions remain hypotheses. The existing sorcin refinement remains rooted in the independently inspected original human 1–121 fragment experiment from PMID:9268363, with the new reconstitution attached as separate corroboration.
PMID:25540196(https://pmc.ncbi.nlm.nih.gov/articles/PMC4335235/) remains abstract-only in the unchanged normal cache. Its complete abstract identifies ALG-2 as the bridge to Sec31A and reports accelerated ER-to-Golgi transport after depletion; neither a reversed transport phenotype nor a direct ANXA11–Sec31A adaptor claim is introduced. PMID:42364743(https://pubmed.ncbi.nlm.nih.gov/42364743/) remains abstract-only; the explicit C-terminal RNA/lipid co-binding result supports retaining RNA binding without declaring the N-terminus its exclusive site. Full construct/species Methods remain unverified.
The final review preserves all 69 original assertion objects and both alternative products, with the consulted 38 ACCEPT/five MODIFY/four KEEP_AS_NON_CORE/22 UNDECIDED decisions unchanged, plus one directly supported NEW molecular function. Uninspected pair-specific and specialized-proteomic records, phagocytosis participation, PEF1 binding and the precise PE transfer remain uncertain. No PAINT tree/node placement has been invented. Final independent consultation, validation, rendering and source-preservation checks are recorded in the session history and closure receipts.
The original 69 source assertions, both alternative products and the prior NEW protein–membrane adaptor assertion are preserved. Eleven uninspected interaction pairs remain UNDECIDED: a source-body flag does not establish inspection of the pair-specific experiment. CHO1/KIF23 remains a verified but potentially indirect non-core association. No interaction is removed solely because its label is generic.
Four ALG-2 refinements continue to recommend calcium-dependent protein binding. Their reasons now distinguish the original generic assertion from the separate recombinant Anx11N–ALG-2 experiment in PMID:12445460. The source fields are unchanged, and the recommendation does not reattribute that experiment to a later screen or manufacture an additional IPI assertion. The already seeded specific binding annotations remain intact.
The broad membrane row now cites actual human U2OS recruitment to membrane lesions in PMID:42574611, rather than an in-vitro RNP-on-GUV experiment. The NK-cell peptide/table detection remains uninspected and is not represented as newly verified. Specialized extracellular-matrix, melanosome and exosome records still lack equivalent independently read target evidence and retain uncertainty.
Ten nuclear, nucleoplasmic and spindle rows are retained as secondary locations. Their positive observations are not disputed, and no PAINT loss or ancestral misplacement is inferred. In contrast, the two calcium-response rows remain core because regulated membrane recruitment directly expresses the established calcium-dependent membrane-binding mechanism; their existing process term is now represented under that activity.
The actual PMID:15197175 matrix, CHO1, depletion and BFA Results, relevant Discussion and Methods were reread. ANXA11 is a detergent-resistant midbody constituent in human cell lines, and depletion disrupts matrix formation and terminal cell separation. The paper distinguishes this matrix pool from Golgi-derived vesicles: BFA does not abolish the midbody association, and the tested Golgi marker does not costain those structures. The CHO1 association can be direct or indirect, while membrane–microtubule coupling, vesicle fusion and lipid rearrangement are proposed alternatives. Therefore the existing midbody and cytokinetic-process annotations remain ACCEPT in a separate structural core with an explicit mechanistic knowledge gap and no assigned MF. This role is not forced into the RNP–membrane adaptor mechanism. No new process or molecular-function annotation is added.
Independent prospective consultation challenged five initially proposed downgrades and supported this representation; the revised plan preserved cytokinesis and calcium-response acceptance. The agent name alx3_followup identifies the actual independent reviewer and is not a biological reference to ALX3. Historical receipt and history filenames remain unchanged. COMPLETE records completion of adjudication, including honest UNDECIDED outcomes, rather than complete experimental access. Final consultation, validation, rendering and preservation checks are recorded in the newly scaffolded follow-up history.
The three generic ANXA11–ALG-2 records from PMID:18256029, PMID:25910212 and PMID:31515488 now remain UNDECIDED. Their source-local pair or construct experiments have not been adjudicated. Although the independent recombinant experiment in PMID:12445460(https://pubmed.ncbi.nlm.nih.gov/12445460/) establishes calcium-dependent binding, it cannot establish what those three original experiments measured. Their earlier cross-paper MODIFY recommendations are superseded; the original generic terms, evidence codes, references and partners remain unchanged. This correction does not deny the interactions or claim that the source papers lacked calcium-dependent assays. Positive calcium evidence remains attached to the annotations supported by the papers that directly report it.
The generic binding record from PMID:12445460 still refines to calcium-dependent protein binding on its own experimental evidence. Its applied replacement should coalesce with the existing same-term, same-paper, same-evidence, same-partner annotation, preserving both original audit entries without counting an additional functional assertion. No valid experimental annotation is removed solely for genericity or duplication.
All 69 original source assertions, both products, the prior NEW membrane-adaptor assertion and all three core functions are preserved. The final action census is 28 ACCEPT, 14 KEEP_AS_NON_CORE, 2 MODIFY and 25 UNDECIDED, plus one previously proposed NEW. COMPLETE continues to mean completed adjudication, including explicit uncertainty. No cache or prior history is changed; final independent consultation and validation are recorded in the new follow-up history.