The Sec15B identity is important throughout this review. EXOC6B/Q9Y2D4 is distinct from EXOC6/Sec15A. A generic historical “Sec15” label is sufficient for neither a paralog-specific interaction nor an identical human mechanism. The displayed 811-residue sequence and the separate 672-residue UniProt product remain as supplied; the experiments below do not establish functional equivalence of those products.
The actual PANTHER PTHR12702 tree places human EXOC6B at PTN002489451 under PTN000294823. The ungapped target MSA equals all 811 residues of the official displayed sequence. Current PAINT IBD rows support exocyst and exocytosis at that ancestor, with no NOT assertion on the target path. The exocyst donor set agrees with the imported source. The current exocytosis IBD lists yeast and Dictyostelium, whereas the imported GOA WITH also lists the worm source. Both versions are preserved; this difference does not demonstrate functional loss or invalidate the target's ancestry.
Official identifiers were traced for all five exocyst donors: AT3G56640/SEC15A/Q9LXX6, AT4G02350/SEC15B/F4JHH5, fly Sec15/Q9VDE6/FBgn0266674, yeast SEC15/P22224/S000003202, and Dictyostelium exoc6/Q54B27/DDB_G0293936. The frozen worm source WBGene00016188 maps to Q18286/sec-15. Only the original studies identified below were independently read; the remaining donor records are database provenance, not a claim of exhaustive primary-paper review.
The current InterPro IPR007225 record explicitly maps intracellular protein transport and Golgi-to-plasma-membrane transport. Its actual Q9Y2D4 match spans residues 5–804. These annotations describe different aspects: protein cargo versus a transport route. The current ontology does not place GO:0006893 below GO:0006886 by is_a/part_of, and its definition says that Golgi-to-plasma-membrane transport precedes exocytosis. Retaining both supported facets avoids an unjustified lateral substitution. Exocytosis itself includes vesicle tethering/docking and kiss-and-run release in its current definition.
The current yeast donor record retains exocytosis PMID:6996832 and Golgi-to-plasma-membrane transport PMID:7026045. Their operative original bodies were not recovered in this lane; the conserved inference is assessed with the valid PAINT/InterPro placement, the independently read assembly/discharge originals above, and the full review below. A current donor entry alone is not described as an independently repeated experiment.
The complete main text, Table 1 and Figure 1 caption of PMID:22420621(https://pmc.ncbi.nlm.nih.gov/articles/PMC3374049/) were read. Its normal cache remains abstract-only and unchanged. This review supports a broad exocyst role across species, discusses fission-yeast Sec8-dependent cell separation, and cites the mammalian centriolin study for midbody/abscission. Its table identifies centriolin–Sec15 without distinguishing Sec15A from Sec15B.
The cited PMID:16213214(https://doi.org/10.1016/j.cell.2005.07.027) original was recovered as a complete reproduced Cell article within a thesis PDF. PDF page 76/printed thesis page 70 identifies the article and describes a contribution to Figure 1. PDF pages 77–89 reproduce original Cell pages 75–87. Original pages 75, 77–79, 81 and 86–87 were selectively read, with Figures 2, 3, 4 and 6 pixels inspected. The article reports:
The inspected main Methods/Results do not supply the recovered sec15 accession or distinguish the two human paralogs. The Sec15 antibody is referred to Yeaman 2003; the listed siRNA coordinates are for Sec5, Sec8 and snapin, not Sec15. Supplementary Figure S1 and movies were not accessed. These are positive human Sec15/exocyst observations, but their EXOC6B-specific attribution remains unresolved. Both assertions remain UNDECIDED. Cytokinesis has positive process evidence with unresolved paralog attribution. Membrane fission has a second uncertainty: the paper places vesicle delivery/fusion before cell cleavage, without identifying an exocyst-performed step in scission. A structural or cofactor contribution could count as participation, but necessity for cytokinesis alone does not establish it.
An additional naming boundary comes from PMID:15292201(https://doi.org/10.1074/jbc.M402264200): actual publisher-indexed Discussion explicitly distinguishes the Rab11-assayed Sec15 from KIAA0919/Sec15B. Selected Results were available, but the complete original and PDF remained inaccessible. Its direct Rab11 activity is not assigned to EXOC6B through the shared Sec15 name. No universal negative about EXOC6B–Rab11 binding is inferred.
The normal publication caches were not rewritten to incorporate these separately recovered originals. Six additional normal records were genuinely fetched: the four recovered/boundary sources 7615633, 22323285, 16213214 and 15292201, plus the original donor-source traces 6996832 and 7026045. All prior normal and runtime preimages were checked. Review-level access flags reflect the actual available originals: complete PMC review and donor originals, complete reproduced Cell main article, and only partial publisher-indexed access for 11406615/15292201. The two older yeast source traces remain explicitly unverified at the operative-paper level. No publication quotations were added. The interaction contexts are covered below using their own original experimental and partner data.
The four imported interaction contexts are positively supported: EXOC5 (O00471) in three studies and SHTN1 product A0MZ66-4 in HuRI. Current UniProt identifies these partners as human EXOC5 and shootin-1, respectively. The supported generic binding assertions remain non-core under the campaign curation instructions; no more specific pair activity is established by these screens. No publication quotations are added.
Boldt et al., PMID:27173435 describes human constructs expressed in HEK293T, StrepII/FLAG tandem-affinity purification and mass spectrometry. The actual Methods and Results were read, including cloning, sequence verification, purification, human database matching and socioaffinity calculation. The scoring combines bait–prey and shared-complex evidence; it is not itself an isolated binary-affinity measurement.
The original supplementary files were obtained from the official BioStudies S-EPMC4869170 archive. In Supplementary Data 1, worksheet “SF-TAP tagged proteins”, rows 84–85 supply the actual EXOC6B coding sequences. Translation gives canonical residues 2–811 for the N-terminally tagged insert and exactly current Q9Y2D4 residues 1–811 for the C-terminally tagged insert. These are cloning/tag boundaries, not additional natural products. Row 82 describes the EXOC5 bait.
Supplementary Data 2, worksheet “tap_purifications”, rows 18414–18415 recover EXOC6B with EXOC5 bait; rows 18915–18918 recover EXOC5 with EXOC6B bait in four experiments. Supplementary Data 3, row 11, contains the significant EXOC6B–EXOC5 pair. Thus the pair is supported by actual reciprocal purification records, not only by an expanded database edge. This does not distinguish every direct molecular contact in the complex or measure membrane tethering. No figure pixels or additional supplementary experiments were inspected.
Luck et al., PMID:32296183 was read in its original Results on the reference interactome and verification workflow. The separately archived HuRI PSI download contains six EXOC6B–EXOC5 records and three EXOC6B–SHTN1 records, spanning array, prey-pooling and validated-two-hybrid methods. Human EXOC6B is labelled Q9Y2D4-1, ORF 100063937; EXOC5 is O00471, ORF 11248; SHTN1 is specifically A0MZ66-4, ORF 15060. The records identify human proteins as GAL4 fusions tested in yeast. Both bait orientations occur among the EXOC5 records.
Current IntAct target records independently retain these pairs under PMID:32296183, using unsuffixed Q9Y2D4. This current-versus-archived accession representation is preserved; historical Ensembl and ORF identifiers do not independently verify the complete present-day clone sequence. The original Results describe quadruplicate retesting and sequence confirmation. Its aggregate MAPPIT/GPCA comparison is not evidence that either specific pair received those orthogonal tests. Full original Methods and supplementary validation tables remain unavailable/unread; no figure inspection or endogenous human-neuron assay is claimed.
Huttlin et al., PMID:33961781 was read in the original Results and operative Methods. Human ORFeome constructs carry C-terminal FLAG-HA tags; anti-HA purification and mass spectrometry were performed separately in HEK293T and HCT116. In the original BioPlex interaction datasets, the 293T network row 103345 contains Q9Y2D4–O00471 with pInt 0.999998779762378. No corresponding pair was found in the inspected HCT116 network; that absence is not a negative localization or binding experiment. Current IntAct independently records the same 293T-study association.
The network supports cellular association and may include indirect complex contacts. The undirected table does not by itself establish a recruitment direction. Its historical protein identifiers and general clone-selection procedure do not prove a particular present-day alternative product. No purified pair affinity, autonomous membrane tethering, pair-specific functional rescue or figure-pixel inspection is claimed.
The genuine UniProt record distinguishes the 811-residue Q9Y2D4-1 and 672-residue Q9Y2D4-2 products. The Boldt insert comparison directly supports its tested long-sequence constructs; the HuRI labels and BioPlex protein groups have the separate limits above. None of these interaction records establishes activity of the short product. EXOC5's exocyst membership and SHTN1's cytoskeletal roles are not automatically activities of EXOC6B. The reviewed sources do not justify replacing these pair assertions with an exocyst-complex cellular-component term or with a specific adaptor, catalytic or tethering activity.
The single core assigns a contribution to the exocyst's membrane-tethering activity, not an isolated EXOC6B activity. The current MF definition describes bridging vesicle and target membranes before docking/fusion. Exocyst GO:0000145 is a vesicle tethering complex; its complex ancestry and capable-of relation support the activity at the assembled-complex level. Protein cargo transport, the Golgi-to-plasma-membrane route and exocytosis are pairwise non-ancestral in the captured current is_a/part_of graph and describe different aspects of this one transport role.
| Source | Operative locator and positive scope | Boundary |
|---|---|---|
| 27173435 | Methods; Supplementary Data 1 construct rows 84–85, Data 2 reciprocal EXOC5/EXOC6B purifications, Data 3 association row 11 | Human HEK293T cellular association and verified 811-residue/2–811 inserts; no isolated tethering assay or 672-product equivalence |
| 11406615 | Publisher-indexed Experimental Procedures, Table I and KIAA0919 Results | Sheep-brain Sec15B peptide identification with historical human sequence matching and rat comparisons; RalA-binding subunit unresolved |
| 7615633 | Original Methods, assembly Results and Figures 2–4 | Yeast Sec6/Sec8/Sec15 co-fractionation and controlled co-immunoprecipitation; no human reconstitution or Sec15-specific bud-tip imaging claim |
| 22323285 | Original Results and Figures 3–6; Dictyostelium culture, imaging and immunoprecipitation Methods | Tagged Sec15/Sec8 incorporation and recruitment at membrane-contact/discharge sites; no human EXOC6B GEF, direct lipid bridge or universal Rab specificity follows |
| 36150098 | Original cell/RNA/protein/cilia Methods, family Results and Figures 3–4; figures inspected | Patient 1 provides protein-loss/cilia measurements; patient 2 provides transcript/RNA-seq and osteogenic differentiation. Cilium frequency is not uniformly reduced. No rescue or natural-product comparison establishes the transport mechanism |
| 38305850 | Actual abstract and publisher Figures 1–5 captions | Mouse ATDC5 model. Full Methods/Results and figure pixels unavailable; no verified human insert or direct molecular step |
| 42068746 | Original metadata/abstract and clipped publisher Methods/Results; HEK293T and HG23270-UT construct entry | Full article, figures and supplement unavailable; exact insert/product and the complete flux/mechanistic controls unresolved. Used for the turnover question only |
The accepted source-specific cytokinesis and membrane-fission decisions remain unresolved because the inspected human Sec15 article does not distinguish the paralog/construct accession. They are not negative-function conclusions. The core has no dedicated ciliary, cytokinetic or autophagy unit, and no such NEW annotation is introduced. The broader exocyst review remains contextual rather than a substitute for the operative original assays above.
Normal publication records are immutable, including records whose automatic full-text or publication-type metadata overstates the reading scope. The manual reference reviews state the actual access. Three already acquired recent papers join the selected citation set; the remaining acquisition-only papers remain private. Genuine GOA and UniProt inputs are separate delivery items, compared against the fixed main preimages and checked again by ROOT at publication.
The preserved UniProt record, CC:FUNCTION and CC:SUBUNIT, supports exocyst membership and vesicle targeting at plasma-membrane fusion sites. Current tethering activity concerns the initial membrane bridge; docking activity concerns stable attachment in close apposition. The exocyst definition identifies a tethering complex. Its contribution is supported; the older broad docking wording does not independently establish the distinct docking MF for EXOC6B.
PMID:36150098(https://pmc.ncbi.nlm.nih.gov/articles/PMC7615863/) is now cited in the exocytosis row and core as human disease context. The abstract describes abrogated exocytosis, but the conclusion says depletion likely impairs it. Main Methods/Results document RNA, protein, cilia and osteogenic measurements; no direct secretion-flux or membrane-fusion assay was identified. Patient 1 supplies the protein-loss/cilia result and patient 2 the RNA-seq/osteogenic result. The reference does not replace the independent complex and evolutionary evidence with a claimed human transport measurement.
A current human comparator query for cilium assembly GO:0060271 and descendants returns one EXOC4/Q96A65 transferred IEA assertion (GO_REF:0000107), and none for EXOC5/O00471 or EXOC6/Q8TAG9. This small, human-only comparison is mixed: it establishes neither a universal exclusion convention nor a missing EXOC6B assertion. The ciliary findings remain biologically relevant, while the particular EXOC6B cargo-delivery step and rescue mechanism remain unresolved; no NEW term is manufactured from comparator presence or absence.
The Cell article used for cytokinesis was read as a third-party thesis reproduction. The access flag records available main text; the provenance and lack of publisher-copy authentication remain explicit. Its delivery/fusion model does not by itself locate the exocyst in the subsequent scission step.