Evidence map›Paper›PMID 28500727›Full record

ReviewJournal of cellular physiology2018

Biological function and histone recognition of family IV bromodomain-containing proteins.

Jonathan T Lloyd, Karen C Glass

Abstract readReview
In one paragraph

Review in Journal of cellular physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

49 citing papers in PubMed, 84 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Jonathan T LloydDepartment of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, Colchester, Vermont.
Karen C GlassDepartment of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, Colchester, Vermont.ORCID http://orcid.org/0000-0002-2761-733X
Albany College of Pharmacy and Health Sciences · US

Funding

Mechanisms of chromatin binding and selection by family IV bromodomainsR15GM104865 · NIGMS · ALBANY COLLEGE OF PHARMACY · PI GLASS, KAREN CHAMPAGNE · 2013 to 2016
$910k
NIGMS NIH HHS R15 GM104865
6 · The paper itself

Abstract

Bromodomain proteins function as epigenetic readers that recognize acetylated histone tails to facilitate the transcription of target genes. There are approximately 60 known human bromodomains, which are divided into eight sub-families based on structural conservation. The bromodomain-containing proteins in family IV include seven members (BRPF1, BRPF2, BRPF3, BRD7, BRD9, ATAD2, and ATAD2b). The bromodomains of each of these proteins recognize and bind acetyllysine residues on histone tails protruding from the nucleosome. However, the histone marks recognized by each bromodomain protein can be very different. The BRPF1 subunit of the MOZ histone acetyltransferase (HAT) recognizes acetylated histones H2AK5ac, H4K12ac, H3K14ac, H4K8ac, and H4K5ac. While the bromodomain of BRD7, a member of the SWI/SNF complex, was shown to preferentially recognize acetylated histones H3K9ac, H3K14ac, H4K8ac, H4K12ac, and H4K16ac. The bromodomains of BRPF2 and BRPF3 have similar sequences, and function as part of the HBO1 HAT complex, but there is limited data on which histone ligands they bind. Similarly, there is little known about the histone targets of the BRD9 and ATAD2b bromodomain proteins. Interestingly, the ATAD2 bromodomain was recently shown to preferentially bind to the di-acetylated H4K5acK12ac mark found in newly synthesized histones following DNA replication. However, despite the physiological importance of the family IV bromodomains, little is known about how they function at the molecular or atomic level. In this review, we summarize our understanding of how family IV bromodomains recognize and select for acetyllysine marks and discuss the importance of acetylated histone recognition for their biological functions.

Indexed as

AcetylationAdaptor Proteins, Signal TransducingATPases Associated with Diverse Cellular ActivitiesBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsEpigenomicsHistone AcetyltransferasesHistone ChaperonesHistonesHumansModels, MolecularNuclear ProteinsProtein BindingTranscription FactorsAdaptor Proteins, Signal TransducingATAD2 protein, humanATPases Associated with Diverse Cellular ActivitiesBRD1 protein, humanBRD7 protein, humanBRD9 protein, humanBromodomain Containing ProteinsBRPF1 protein, humanChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistone AcetyltransferasesHistone ChaperonesHistonesNuclear ProteinsTranscription Factorsacetyllysinebromodomainchromatin reader domainepigeneticshistone

Identifiers

PMID28500727
PMCPMC5683942
OpenAlexW2612603429

What OpenQuestion holds

Textmetadata
LicenceTDM
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.