Evidence map›Paper›PMID 7623795›Full record

ArticleMolecular and cellular biology1995

Cooperative interactions between HOX and PBX proteins mediated by a conserved peptide motif.

M L Phelan, I Rambaldi, M S Featherstone

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
7.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

79 citing papers in PubMed, 223 citations in OpenAlex.

  1. Article
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  4. Diversification and Functional Evolution of HOX Proteins.Frontiers in cell and developmental biology · 2022
    Review
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  18. Article
  19. Pbx homeodomain proteins: TALEnted regulators of limb patterning and outgrowth.Developmental dynamics : an official publication of the American Association of Anatomists · 2011
    Review
  20. Article

19 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

M L PhelanMcGill Cancer Centre, McGill University, Montreal, Québec, Canada.
I Rambaldi
M S Featherstone
McGill University Health Centre · CAMcGill University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homeoprotein products of the Hox/HOM gene family pattern the animal embryo through the transcriptional regulation of target genes. We have previously shown that the labial group protein HOXA-1 has intrinsically weak DNA-binding activity due to residues in the N-terminal arm of its homeodomain (M. L. Phelan, R. Sadoul, and M. S. Featherstone, Mol. Cell. Biol. 14:5066-5075, 1994). This observation, among others, suggests that HOX and HOM proteins require cofactors for stable interactions with DNA. We have demonstrated that a putative HOX cofactor, PBX1A, participates in cooperative DNA binding with HOXA-1 and the Deformed group protein HOXD-4. Three Abdominal-B class HOX proteins failed to cooperate with PBX1A. We mapped the interacting domain of HOXD-4 to the YPWMK pentapeptide motif, a conserved sequence found N terminal to the homeodomain of HOXA-1 and many other homeoproteins but absent from the Abdominal-B class. The naturally occurring fusion of the transcriptional activation domain of E2A with PBX1 creates an oncoprotein implicated in human pre-B-cell leukemias (M. P. Kamps, C. Murre, X.-H. Sun, and D. Baltimore, Cell 60:547-555, 1990; J. Nourse, J. D. Mellentin, N. Galili, J. Wilkinson, E. Starbridge, S. D. Smith, and M. L. Cleary, Cell 60:535-545, 1990). A pentapeptide mutation that abolished cooperative interaction with PBX1A in vitro also abrogated synergistic transcriptional activation with the E2A/PBX oncoprotein. The direct contact of PBX family members by the HOX pentapeptide is likely to play an important role in developmental and oncogenic processes.

Indexed as

Conserved SequenceTranscription, GeneticAmino Acid SequenceBase SequenceDNADNA-Binding ProteinsGene Expression Regulation, NeoplasticHomeodomain ProteinsHumansMolecular Sequence DataOncogene Proteins, FusionPeptide FragmentsPre-B-Cell Leukemia Transcription Factor 1Protein BindingProtein ConformationProto-Oncogene ProteinsDNADNA-Binding ProteinsE2A-Pbx1 fusion proteinHomeodomain ProteinsHOXD10 protein, humanOncogene Proteins, FusionPBX1 protein, humanPeptide FragmentsPre-B-Cell Leukemia Transcription Factor 1Proto-Oncogene ProteinsTranscription Factors

Identifiers

PMID7623795
PMCPMC230638
OpenAlexW2139128323

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.