Evidence map›Paper›PMID 27151440›Full record

ArticleMolecular cell2016

PRDM16 Suppresses MLL1r Leukemia via Intrinsic Histone Methyltransferase Activity.

Bo Zhou, Jingya Wang, Shirley Y Lee, Jie Xiong, Natarajan Bhanu, Qi Guo, Peilin Ma, Yuqing Sun, Rajesh C Rao, Benjamin A Garcia and 2 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 69 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

12 authors at 2 institutions in 1 country.

Bo ZhouDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Jingya WangDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Shirley Y LeeDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Jie XiongDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Natarajan BhanuDepartment of Biochemistry and Biophysics, Smilow Center for Translational Research, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-5157, USA.
Qi GuoDepartment of Biochemistry and Biophysics, Smilow Center for Translational Research, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-5157, USA.
Peilin MaDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Yuqing SunDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Rajesh C RaoDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA; Ophthalmology & Visual Sciences, University of Michigan, Ann Arbor, MI 48109, USA.
Benjamin A GarciaDepartment of Biochemistry and Biophysics, Smilow Center for Translational Research, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-5157, USA.
Jay L HessDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Yali DouDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: yalid@umich.edu.
University of Michigan · USUniversity of Pennsylvania · US

Funding

Function of MLL in transcription regulationR01GM082856 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI DOU, YALI · 2009 to 2023
$4.0M
New Therapeutic Targets in AMLR01CA151425 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI HESS, JAY L. · 2011 to 2015
$1.7M
Understanding the Role of Combinatorial Histone PTM PatternsR01GM110174 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GARCIA, BENJAMIN A · 2014 to 2017
$1.3M
NCI NIH HHS R01 CA151425NIGMS NIH HHS R01 GM082856NIGMS NIH HHS R01 GM110174
6 · The paper itself

Abstract

PRDM16 is a transcription co-factor that plays critical roles in development of brown adipose tissue, as well as maintenance of adult hematopoietic and neural stem cells. Here we report that PRDM16 is a histone H3K4 methyltransferase on chromatin. Mutation in the N-terminal PR domain of PRDM16 abolishes the intrinsic enzymatic activity of PRDM16. We show that the methyltransferase activity of PRDM16 is required for specific suppression of MLL fusion protein-induced leukemogenesis both in vitro and in vivo. Mechanistic studies show that PRDM16 directly activates the SNAG family transcription factor Gfi1b, which in turn downregulates the HOXA gene cluster. Knockdown Gfi1b represses PRDM16-mediated tumor suppression, while Gfi1b overexpression mimics PRDM16 overexpression. In further support of the tumor suppressor function of PRDM16, silencing PRDM16 by DNA methylation is concomitant with MLL-AF9-induced leukemic transformation. Taken together, our study reveals a previously uncharacterized function of PRDM16 that depends on its PR domain activity.

Identifiers

PMID27151440
PMCPMC5061593
OpenAlexW2338231408

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.