Evidence map›Paper›PMID 17698583›Full record

ArticleMolecular and cellular biology2007

Species selectivity of mixed-lineage leukemia/trithorax and HCF proteolytic maturation pathways.

Francesca Capotosti, James J-D Hsieh, Winship Herr

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
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

37 citing papers in PubMed.

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  10. Catalytic deficiency of O-GlcNAc transferase leads to X-linked intellectual disability.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Effects of hypo-The Journal of biological chemistry · 2018
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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.

Francesca CapotostiCenter for Integrative Genomics, University of Lausanne, Génopode Building, 1015 Lausanne, Switzerland.
James J-D Hsieh
Winship Herr

Funding

Molecular Mechanisms of Impaired DAN Damage Response in Leukemia PathogenesisR01CA138505 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI HSIEH, JAMES J · 2013 to 2015
$1.0M
NCI NIH HHS R01 CA138505
6 · The paper itself

Abstract

Site-specific proteolytic processing plays important roles in the regulation of cellular activities. The histone modification activity of the human trithorax group mixed-lineage leukemia (MLL) protein and the cell cycle regulatory activity of the cell proliferation factor herpes simplex virus host cell factor 1 (HCF-1) are stimulated by cleavage of precursors that generates stable heterodimeric complexes. MLL is processed by a protease called taspase 1, whereas the precise mechanisms of HCF-1 maturation are unclear, although they are known to depend on a series of sequence repeats called HCF-1(PRO) repeats. We demonstrate here that the Drosophila homologs of MLL and HCF-1, called Trithorax and dHCF, are both cleaved by Drosophila taspase 1. Although highly related, the human and Drosophila taspase 1 proteins display cognate species specificity. Thus, human taspase 1 preferentially cleaves MLL and Drosophila taspase 1 preferentially cleaves Trithorax, consistent with coevolution of taspase 1 and MLL/Trithorax proteins. HCF proteins display even greater species-specific divergence in processing: whereas dHCF is cleaved by the Drosophila taspase 1, human and mouse HCF-1 maturation is taspase 1 independent. Instead, human and Xenopus HCF-1PRO repeats are cleaved in vitro by a human proteolytic activity with novel properties. Thus, from insects to humans, HCF proteins have conserved proteolytic maturation but evolved different mechanisms.

Indexed as

Amino Acid SequenceAnimalsChromosomal Proteins, Non-HistoneDrosophila melanogasterDrosophila ProteinsEndopeptidasesEnzyme StabilityEvolution, MolecularHeLa CellsHumansMiceMolecular Sequence DataMyeloid-Lymphoid Leukemia ProteinProtease InhibitorsProtein PrecursorsRNA InterferenceChromosomal Proteins, Non-HistoneDrosophila ProteinsEndopeptidaseshost cell factor, DrosophilaMyeloid-Lymphoid Leukemia ProteinProtease InhibitorsProtein Precursorstaspase1, Drosophilataspase1, humantrx protein, Drosophila

Identifiers

PMID17698583
PMCPMC2168920

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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.