EIF4G1 (Q04637) - a translation-initiation scaffold in the pan-MLL-fusion core, alone, with no other eIF4F subunit anywhere in the 960
also called EIF4G1 · eIF4G · eIF4GI · eIF4G1 · EIF4F · EIF4G · p220 · IF4G1_HUMAN · Q04637
eIF4G1 is the big scaffold protein that assembles the machinery which starts protein synthesis, a job done in the cytoplasm. It nevertheless turned up attached to all seven MLL fusion proteins in a nuclear extract - and, oddly, none of the other parts of that machinery came with it, which is the opposite of what an accidental contamination by the translation apparatus would look like.
The same thing, for a scientist
eIF4G1 (Q04637, 1,599 aa) is the scaffold of the eIF4F cap-binding complex. It co-purified with all seven Strep-HA-tagged MLL fusions in Skucha 2018 (MLL-AF4 p = 0.0448, 7|2, negative control 0|0, rank 33 of 42) and is in the post-filter 128 and the shRNA library. The measurement that makes this entry more than a dismissal: **EIF4G2, EIF4G3, EIF4A1, EIF4E, EIF3A and PABPC1 are ALL absent from the 960-protein network at any n**, checked against the full table on 2026-09-21. There is no eIF4F module and no translation module. A prep contaminated by the translation apparatus would bring ribosomal proteins and PABP; this one brings a single 1,599-residue scaffold. UniProt records a nuclear pool on ECO:0000269, and this beat did what rule 91 requires and read the cited paper rather than trusting the pointer - the abstract is entirely about cytoplasmic stress granules and describes no nuclear experiment, but the full text does: Figure 2A, a goat anti-eIF4GI antibody localises the protein 'to the cytoplasm and nucleus' in COS7 cells. That is a real experiment invisible from the abstract, which is rule 80 firing in the direction that rescues rather than condemns. The nuclear pool is therefore established but on a single incidental immunofluorescence panel.
The Skucha row, stated in full
7 of 7 fusions. MLL-AF1p 9.74e-05 (12|7), MLL-AF4 0.0448 (7|2), MLL-AF9 5.48e-05 (15|17), MLL-CBP 0.00697 (6|6), MLL-EEN 0.00036 (22|15), MLL-ENL 4.4e-06 (18|22), MLL-GAS7 1.63e-08 (37|31); negative control 0|0 1. Rank 33 of 42 by MLL-AF4 p. The MLL-AF4 spectral total of 9 is rank 7 of the seven baits against 68 under MLL-GAS7 - and note that MLL-GAS7, the deepest bait for this prey, is the one whose partner is an F-BAR actin-binding protein.
The isolation argument, which points the unexpected way
Checked against the full 960-row table on 2026-09-21: EIF4G2, EIF4G3, EIF4A1, EIF4E, EIF3A, PABPC1, RPS3 and EEF1A1 are all absent. EEF2 is present at n = 2 and RPL10A at n = 3, neither with an MLL-AF4 value. So there is no translation module in this network at all, and eIF4G1 is not travelling with its own complex.
This cuts against the lazy reading. If the nuclear prep were carrying the translation apparatus as bulk cytoplasmic carryover, PABPC1 and the abundant initiation and elongation factors would be the first things to appear, and they are not there. What is there is one very large scaffold protein. That does not make the interaction real - eIF4G1 is abundant and large, and large proteins yield more tryptic peptides and therefore more spectra for the same molar amount - but it does mean the simplest contamination story does not fit 1.
The nuclear pool: a rule-91 check that came out the other way
UniProt Q04637 carries 'Nucleus' at ECO:0000269 on PubMed 17984221 - and the same PMID carries 'Cytoplasm'. Rule 91 says open the cited paper and check it is about your fact. Its title is Proline-rich transcript in brain protein induces stress granule formation and its abstract is entirely about cytoplasmic stress granules; nothing nuclear appears in it. That is the shape of a wrong pointer, and this beat nearly recorded it as one.
Rule 80 says look in the figures, and the experiment is there. The full text, reached through the PMC HTML route after fullTextXML returned HTTP 500, contains: 'Using a goat antibody against eIF4GI, the eIF4GI protein also was shown to localize to the cytoplasm and nucleus (Fig. 2A, image b).' So UniProt's coded annotation is legitimate. The finding is recorded at the strength it deserves - a single incidental immunofluorescence panel with a goat polyclonal in COS7 (monkey) cells, not a fractionation and not the paper's subject 2.
eIF4E is in this graph and is not in this network
This graph already holds localization-hoxa9-nuclear-bodies-and-the-eif4e-body-switch: in FAB M4/M5 AML and blast-crisis CML, HOXA9 colocalises with abnormally enlarged eIF4E nuclear bodies. eIF4E is eIF4G1's direct binding partner and the reason eIF4G1 exists. So the graph already contains a documented nuclear-body compartment for the other half of this pair, in AML marrow, with HOXA9 in it - and EIF4E is absent from the Skucha 960 at any n. Those two facts sit next to each other and nobody has looked at them together. This entry records the juxtaposition as an open question and asserts nothing from it.
Verdict
Undecidable, leaning artefact, but for a different reason than the rest of the tranche. Against: a p of 0.0448 that barely clears the conventional line, the lowest bait depth of the seven, an abundant protein whose size inflates spectral counts, and no independent tie to any KMT2A fusion (EIF4G1[tiab] and eIF4G[tiab] against the KMT2A clause both return 0). For: a genuinely documented nuclear pool, and the absence of any eIF4F or ribosomal company, which removes the obvious contamination mechanism.
| uniprot | Q04637 |
|---|---|
| length AA | 1599 |
| accession resolution | Resolved live 2026-09-21: `gene_exact:EIF4G1 AND organism_id:9606 AND reviewed:true` returns exactly ONE reviewed row; gene_primary EIF4G1, Q04637, entry name IF4G1_HUMAN, 1,599 aa, protein name 'Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (p220)', synonyms EIF4F EIF4G EIF4GI. Matches the accession in Skucha's own table. |
| identifier hazard | REAL, NOT IN data/symbol-collisions.json AS OF 2026-09-21 (registry read before searching, per rule 88), AND A ROW IS WARRANTED. Two traps. (1) `EIF4F` is a curated GENE SYNONYM of EIF4G1 in UniProt, but in the literature eIF4F is the NAME OF THE THREE-SUBUNIT COMPLEX (eIF4E + eIF4A + eIF4G). A search or an automated resolver that treats EIF4F as this gene will collect a complex-level literature and attribute it to one subunit - the same shape as rule 64's FACT/CHUK problem, running in reverse. (2) `EIF4G` without a number is ambiguous between EIF4G1 (Q04637, 1,599 aa) and EIF4G3 (O43432) and, loosely, EIF4G2/DAP5 (P78344); older papers use the bare form. Length IS a defence in this family. Rule 65 readback SUCCEEDS - the protein name contains eIF-4G 1. |
| localization | CYTOPLASM AND NUCLEUS, the nuclear call resting on one figure panel. UniProt Q04637, fetched live 2026-09-21 with per-location evidence codes read individually: 'Cytoplasm' ECO:0000269 PubMed:17984221; 'Nucleus' ECO:0000269 PubMed:17984221 (the SAME citation for both); 'Cytoplasm, Stress granule' ECO:0000269 PubMed:22872150. The cited paper was fetched and read by this beat rather than taken on UniProt's pointer (rule 91). Its abstract describes no nuclear experiment; its Figure 2A does - 'the eIF4GI protein also was shown to localize to the cytoplasm and nucleus', by goat-polyclonal immunofluorescence in COS7 cells. The pointer is therefore correct and the underlying evidence is thin. |
| subnuclear localization | NOT ESTABLISHED, and this is a genuine gap rather than a not-applicable: eIF4G1 has an experimentally supported nuclear pool, so the subnuclear question is meaningful for it. UniProt records no subnuclear compartment. The nearest relevant compartment in the literature is the eIF4E NUCLEAR BODY, which this graph already holds for HOXA9 in FAB M4/M5 AML and blast-crisis CML marrow - and eIF4E is eIF4G1's direct partner. Whether eIF4G1 is in those bodies has not been asked. This entry deliberately does NOT infer a compartment from a named partner. |
| localization shown for fusion | NO - nobody has imaged or fractionated eIF4G1 in any cell expressing any KMT2A fusion. |
| shown for fusion | Co-purification with all seven MLL fusions including MLL-AF4 in Jurkat (p = 0.0448); shRNA-screened in MLL-AF9 MOLM-13, score unpublished. NO independent experiment ties eIF4G1 to any KMT2A fusion - both symbol queries return 0. |
| selectivity | UNKNOWN, and BARRED from any target list on the evidence in this entry. Not named among the paper's controls and not known to be among the 40 re-screened. Note the separate and genuine fact that cap-dependent translation IS a live therapeutic axis in leukaemia (eIF4E, 4E-BP1, MNK inhibitors) - that literature is not about this interaction, and nothing here should be used to support it. The paper's own SF3A3 precedent applies: a pan-fusion protein can be a named NON-selectivity control. |
| absence class | never-measured |
| absence class note | No instrument has been pointed at eIF4G1 in a KMT2A-rearranged cell outside the two screen hosts. The MOLM-13 shRNA score is measured-not-reported. PRIDE checked: PXD009338 is the only relevant deposition. |
| graph context | EIF4G1 appears in ZERO of this graph's 1,924 node files before this entry. Its direct partner eIF4E does appear, in `localization-hoxa9-nuclear-bodies-and-the-eif4e-body-switch`. |
| verdict | UNDECIDABLE, LEANING ARTEFACT - but on different grounds from the rest of the tranche. The contamination story is weakened by the complete absence of the eIF4F complex, the ribosome and PABPC1 from the network; the interaction story is weakened by a marginal p, the lowest bait depth of the seven, a size-driven spectral-count confound, and a nuclear pool documented by one incidental figure panel. |
skucha 2018
{
"bait": "MLL-AF4 (= KMT2A::AFF1)",
"p_value": 0.0448,
"spectral_counts": "7|2",
"n_fusions_of_seven": 7,
"negative_control_counts": "0|0",
"per_bait": {
"MLL-AF1p": "9.74e-05 (12|7)",
"MLL-AF4": "0.0448 (7|2)",
"MLL-AF9": "5.48e-05 (15|17)",
"MLL-CBP": "0.00697 (6|6)",
"MLL-EEN": "0.00036 (22|15)",
"MLL-ENL": "4.4e-06 (18|22)",
"MLL-GAS7": "1.63e-08 (37|31)"
},
"af4_spectral_rank_of_seven": 7,
"af4_p_rank_within_the_42_pan_fusion": 33,
"source": "analyses/skucha-mll-fusion-interactome/results.json, re-derived from the cached MOESM4 xlsx 2026-09-21; run.py re-run, both controls PASS"
}complex membership
{
"complex": "eIF4F cap-binding complex (eIF4E + eIF4A + eIF4G)",
"partners_in_the_960": {},
"absent_from_the_960": [
"EIF4E",
"EIF4A1",
"EIF4G2",
"EIF4G3",
"EIF3A",
"PABPC1",
"RPS3",
"EEF1A1",
"NPM1"
],
"present_but_marginal": {
"EEF2": "n=2, MLL-AF4 p 0.11 (8|7), neg 0|0",
"RPL10A": "n=3, no MLL-AF4 value, neg 0|0"
},
"reading": "NO MODULE, AND THE ABSENCE IS THE ARGUMENT. Every other eIF4F subunit, the cap-binding protein, the poly(A)-binding protein and the abundant initiation/elongation factors are absent. A nuclear prep carrying the translation apparatus as bulk cytoplasmic carryover would bring those first. It brings one large scaffold instead. This does not establish specificity, but it removes the simplest contamination mechanism. No translation module was tested in analyses/mll-fusion-interactome-complexes/."
}cell types and states
[ "Jurkat (human T-ALL) - the AP-MS host, nuclear lysate, tagged single-copy transgene", "MOLM-13 (human MLL-AF9 AML) - shRNA screen host, six shRNAs, per-gene score unpublished", "COS7 (African green monkey kidney) and HeLa - the localisation and stress-granule work", "no B-lineage cell, no infant cell, and no KMT2A::AFF1 cell of any kind" ]
functionally screened in the source paper
{
"screened": true,
"shrnas_for_this_gene": 6,
"design": "Supplementary Table 6 / MOESM5 is the shRNA library for the negative-selection screen: 768 data rows, 128 unique gene symbols, EXACTLY 6 shRNAs each - counted with openpyxl by this beat on 2026-09-21. Host is MLL-AF9-expressing MOLM-13, a human myeloid line.",
"set_identity_measured_by_this_beat": "The 128 symbols in the shRNA library are the SAME SET as the 128 rows of MOESM4 with n_fusions >= 5, checked by set difference on 2026-09-21: the only four mismatches are alias spellings (JADE2/PHF15, JADE3/PHF16, KMT2A/MLL, NIFK/MKI67IP). This matters for the contamination question. The paper says 'Seven proteins were manually removed as these were either frequently observed contaminants or were not detected in human hematopoietic cell lines. The final set was comprised of 128 proteins.' Because the table's >=5 set is already exactly 128, those seven are NOT recoverable from Supplementary Table 5 - and every protein in this tranche is in the post-removal 128 and was carried into the functional screen.",
"what_this_does_NOT_establish": "A per-gene result. Scores are presented only as heatmaps (Fig. 2c/2d); no per-gene depletion value is tabulated anywhere in the paper or its supplementary files, so for any individual gene the outcome is measured-not-reported. It is also MLL-AF9 MOLM-13, a myeloid line, not the index fusion and not B-lineage.",
"the_filter_is_leaky_and_here_is_the_proof": "'Survived the authors' manual contaminant removal' is weaker than it sounds. CCT3 is also in the 128 and was also screened, and the CCT/TRiC chaperonin is the canonical AP-MS contaminant - the companion analysis analyses/mll-fusion-interactome-complexes/ uses it as its NEGATIVE control and it is still significant against a nuclear background (q = 2.7e-05, 8 of 9 subunits in the MLL-AF4 column). The authors' own named essentiality controls were RFC1, SF3A3 and CCT3. So the manual removal did not remove a canonical contaminant complex, and membership in the 128 is not the authors certifying a protein as a real partner.",
"absence_class_for_the_per_gene_score": "measured-not-reported",
"library_symbol": "EIF4G1"
}bounded literature
{
"query": "EIF4G1[tiab] AND (KMT2A[tiab] OR MLL[tiab] OR \"MLL-AF4\"[tiab] OR \"MLL-AF9\"[tiab] OR \"t(4;11)\"[tiab])",
"querytranslation": "\"EIF4G1\"[Title/Abstract] AND (\"KMT2A\"[Title/Abstract] OR \"MLL\"[Title/Abstract] OR \"MLL-AF4\"[Title/Abstract] OR \"MLL-AF9\"[Title/Abstract] OR \"t 4 11\"[Title/Abstract])",
"count": 0,
"second_query": "eIF4G[tiab] AND the identical KMT2A clause",
"second_querytranslation": "\"eIF4G\"[Title/Abstract] AND (\"KMT2A\"[Title/Abstract] OR \"MLL\"[Title/Abstract] OR \"MLL-AF4\"[Title/Abstract] OR \"MLL-AF9\"[Title/Abstract] OR \"t 4 11\"[Title/Abstract])",
"second_count": 0,
"date": "2026-09-21",
"tool": "NCBI esearch db=pubmed",
"names_tried": [
"EIF4G1",
"eIF4G",
"eIF4GI (covered by the eIF4G stem in PubMed's phrase match? NOT assumed - eIF4G returned 0 on its own and eIF4GI was not separately run, which is a residual gap in this bound)"
],
"positive_control": "MEN1[tiab] AND the identical five-term KMT2A clause returns 85.",
"complex_level_query_not_run": "The complex form - 'eIF4F' or 'cap-dependent translation' against the KMT2A clause - was NOT run, and rule 64 says it should have been. This bound is therefore weaker than the others in this tranche and should be closed by a later beat.",
"bound": "Titles and abstracts only; supporting figures not searched (rule 80). Cytogenetic term quoted, querytranslation read back with no injected [UID] term (rule 95). One tag per term (rule 94)."
}what would settle it
[ "Reanalyse PXD009338 for EIF4E, EIF4A1, EIF4G3 and PABPC1 peptides below the 300-per-bait rank cutoff. If the eIF4F complex is there sub-threshold, the 'no module' argument collapses and this becomes ordinary carryover.", "Is eIF4G1 in eIF4E nuclear bodies? The graph already holds those bodies for HOXA9 in AML marrow; a two-colour immunofluorescence in the same specimens would answer it.", "Run the complex-level bounded query that this entry did not run: 'eIF4F' and 'cap-dependent translation' against the KMT2A clause (rule 64)." ]
- eIF4G1 must not reach a target list from this entry. Global translation initiation has no selective window, and the interaction itself is undecided.
- The specific risk here is a narrative one: 'MLL fusions touch the translation machinery' is an attractive sentence that this single row cannot support, and the absence of every other eIF4F subunit is as easily read as the cutoff truncating a module as it is as specificity.
- If a later beat does find eIF4F sub-threshold in PXD009338, this entry should be downgraded to speculative and say so in the body, not only in counter-evidence.
- Is the eIF4F complex present in PXD009338 below the rank cutoff? The whole 'no module, so not simple carryover' argument in this entry rests on an absence from a rank-truncated list, which is the weakest kind of absence.
- Is eIF4G1 in the eIF4E nuclear bodies this graph already records for HOXA9 in FAB M4/M5 AML? Nobody has looked, and eIF4G1 is eIF4E's obligate scaffold.
- Does spectral counting need a length correction in this table? eIF4G1 at 1,599 aa is the largest prey in this tranche and MAPRE1 at 268 aa the smallest; the paper's GLM does not model peptide count per protein, so the two are not on the same scale.
- Cap-dependent translation is a real therapeutic axis in leukaemia and this graph holds nothing about it. That is a gap this entry notices and does not fill.
- E1weak confidence 2 of 5: Preliminary, small, indirect, or not yet peer reviewed.paper
eIF4G1 co-purified with all seven Strep-HA-tagged MLL fusions from nuclear lysates of isogenic human Jurkat T-ALL cells; for MLL-AF4 (= KMT2A::AFF1) the combined p-value is 0.0448 with spectral counts 7|2 and a negative control of 0|0, and it is in the paper's final post-filter set of 128 that entered the MOLM-13 shRNA screen.
MLL-fusion-driven leukemia requires SETD2 to safeguard genomic integrity. · Skucha A, Ebner J, Schmoellerl J, Roth M, Eder T, Cesar-Razquin A, Stukalov A, Vittori S, Muhar M, Lu B, Aichinger M, Jude J, Mueller AC, Gyorffy B, Vakoc CR, Valent P, Bennett KL, Zuber J, Superti-Furga G, Grebien F · Nature Communications 2018What this evidence cannot show
SYSTEM: the AP-MS host is JURKAT, a human T-ALL line, while KMT2A::AFF1 disease is B-lineage infant leukaemia; a partner requiring a B-cell or infant proteome cannot appear here and a T-lineage partner can appear spuriously. The bait is a Strep-HA-tagged, SINGLE-COPY, doxycycline-induced transgene at an FRT/Flp cassette, not the endogenous fusion. Prey came from bulk nuclear lysate after a single STREP-Tactin step, so co-purification is NOT evidence of a direct contact and is not evidence that the two proteins are ever in the same complex. INCLUSION RULE: the paper kept a fixed number of top-ranked interactions per bait rather than applying a p threshold. Methods, read verbatim from the PMC full text by this beat on 2026-09-21: "All the identified bait-prey pairs were ranked by the combined p-value. The 300 most significant interactions per bait were retained." Measured by this beat from the cached MOESM4 xlsx: within the MLL-AF4 column 186 of 291 listed p-values (63.9%) exceed 0.05, and that column's maximum p is 0.175. BAIT DEPTH: for all nine proteins in this tranche the MLL-AF4 spectral total is rank 7 of the seven baits - measured protein by protein - so a low MLL-AF4 count is a bait property (transgene expression, purification depth, or the GLM normalisation) and must not be read as a weaker association than the same protein's count under another bait. HOW TO READ THE NEGATIVE CONTROL, measured by this beat on 2026-09-21 over all 960 rows of MOESM4: the Spearman correlation between a protein's neg_ctrl spectral total and its maximum per-bait spectral total is +0.461, and the median maximum per-bait spectral count is 42 for the 145 proteins (15.1%) with a non-zero negative control against 8 for the 815 with 0|0. A dirty negative control in this table is therefore substantially a statement about protein ABUNDANCE, not about specificity, and a clean 0|0 is substantially a statement that two control replicates were not deep enough to see the protein at all. Two consequences. (1) PSIP1/LEDGF - the one pan-fusion partner with a solved co-crystal against the KMT2A N-terminus - carries 0|5, the second-dirtiest control of the 42, so a non-zero control cannot be used to call a protein a contaminant. (2) A 0|0 control is not purity; it is an unestimated baseline. The paper's GLM estimates each prey's baseline abundance A0,j from the control purifications, so a prey the controls never saw has its baseline set by a floor rather than by data, which is the direction that inflates apparent specificity. WHERE THIS ROW SITS AMONG THE 42, measured by this beat on 2026-09-21: ranked by MLL-AF4 p-value the pan-fusion set runs from MEN1 at 9.75e-16 to SMC3 at 0.174. The three WEAKEST MLL-AF4 calls in the whole pan-fusion set - SMC3 0.174, NOLC1 0.134, TRIM28 0.129 - all already have entries in this graph, and gene-nolc1 and gene-trim28 both carry confidence_overall 'weak' with those p-values recorded. So p > 0.05 in the index-fusion column is not a disqualifier in this corpus; it is a confidence tier that two existing entries already occupy. SPECIFIC TO THIS PROTEIN, measured by this beat from the cached MOESM4 xlsx on 2026-09-21: MLL-AF4 p = 0.0448, rank 33 of 42 - it clears 0.05 by less than a factor of two, and one of the seven baits' p-values would not. EIF4G2, EIF4G3, EIF4A1, EIF4E, EIF3A, PABPC1, RPS3 and EEF1A1 are ALL absent from the 960 at any n, so there is no eIF4F or translation module - which removes the simplest contamination mechanism and is the main reason this row is not dismissed outright. A SIZE CONFOUND specific to this protein and not corrected in the source paper's model: at 1,599 residues eIF4G1 is the largest prey in this tranche by a factor of two, and spectral counting scales with the number of observable tryptic peptides, so equal molar amounts of eIF4G1 and a 268-residue protein do not give equal counts. SELECTIVITY: not named among the paper's controls (RFC1, SF3A3, CCT3 non-selective; MEN1 selective), not known to be among the unpublished 40 re-screened. Recorded as unknown. run.py re-run 2026-09-21, both controls PASS.
Evidence that argues against this (2)
- The clean 0|0 control carries almost no information: 32 of the 42 pan-fusion proteins (76.2%) have one, and over all 960 rows the control total correlates with maximum per-bait spectral abundance at Spearman +0.461. eIF4G1's maximum per-bait total is 68, mid-range. IntAct has never curated this dataset and the raw spectra at PXD009338 have not been reanalysed here - a reanalysis for EIF4E, EIF4A1 and PABPC1 peptides below the 300-per-bait rank cutoff is the one experiment that would decide whether the 'no module' argument is real or just a cutoff effect. ProteomeXchange/PRIDE 2018
- Translation-initiation factors are among the frequently observed background proteins in affinity purification-mass spectrometry, and the CRAPome authors state that a study's own limited negative controls do not capture a complete background protein set. Skucha 2018 scored against its own controls and consulted no contaminant repository; a CRAPome frequency for Q04637 was not retrieved by this beat and would be the cheapest external check. Mellacheruvu D et al. 2013
- E2weak confidence 2 of 5: Preliminary, small, indirect, or not yet peer reviewed.paper
Indirect immunofluorescence with a goat antibody against eIF4GI shows the endogenous protein localised to both the cytoplasm and the nucleus of COS7 cells under normal conditions; on sodium arsenite treatment some of the cytoplasmic pool redistributes into cytoplasmic stress-granule speckles together with PRTB.
Proline-rich transcript in brain protein induces stress granule formation. · Kim JE, Ryu I, Kim WJ, Song OK, Ryu J, Kwon MY, Kim JH, Jang SK · Mol Cell Biol 2008What this evidence cannot show
THIS IS THE FIGURE, NOT THE ABSTRACT. UniProt Q04637 cites this PMID at ECO:0000269 for BOTH 'Cytoplasm' and 'Nucleus', and the abstract describes only cytoplasmic stress granules - so under rule 91 this looked like a mis-pointed annotation. It is not: the nuclear observation is in Figure 2A, reached by this beat through the PMC HTML route (PMC2223406) after Europe PMC's fullTextXML returned HTTP 500, per the five-route rule. The observation is weak on its own terms: a single incidental immunofluorescence panel, a goat polyclonal, COS7 (African green monkey kidney) cells, no fractionation, no quantification, and nuclear eIF4GI is not what the paper is about. It is not a haematopoietic system and has nothing to do with any fusion. Recorded here because a nuclear pool is the necessary condition for the Skucha row to be possible at all, and because the rule-91/rule-80 sequence that found it is worth preserving.
Evidence that argues against this (1)
- A nuclear pool makes the AP-MS row possible without making it specific. And the same paper's Figure 2 is a reminder of how indirect this is: its actual subject, PRTB, was itself reported as nuclear-speckle by one group and cytoplasmic-speckle by another, and the authors attribute the discrepancy to cell line - 'the proportions of cytoplasmic and nuclear speckles varied by the cell line tested'. A localisation that changes with the cell line is a poor basis for predicting what happens in Jurkat, let alone in an infant B-lineage blast. Skucha A et al. 2018
EIF4G1 is an eIF4F scaffold that does nothing alone, and neither EIF4E nor EIF4A1 is in the network. Consistent with this entry's own observation that no eIF4F component, no ribosome and no PABPC1 appears -- which also means simple translational carryover does not explain it.
co-purified, all 7 MLL fusions, Jurkat nuclear-lysate AP-MS, MLL-AF4 p=0.0448 (7|2), neg 0|0 - undecidable; co-purification only
eIF4E is eIF4G1's obligate partner and has documented nuclear bodies in FAB M4/M5 AML marrow - but EIF4E is absent from the Skucha 960 and nobody has asked whether eIF4G1 is in those bodies
- related to →KMT2A / MLL1 — the gene that breaks
pan-MLL-fusion core prey; the shared bait is the KMT2A N-terminus
the two pan-fusion preys in this tranche recovered WITHOUT any member of their own obligate complex - no PKA catalytic subunit, no other eIF4F subunit - which removes the simplest contamination mechanism for both without establishing either