PMID- 24451260
OWN - NLM
STAT- MEDLINE
DCOM- 20141104
LR  - 20211021
IS  - 1939-4586 (Electronic)
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 25
IP  - 6
DP  - 2014 Mar
TI  - Transcriptional repression of hypoxia-inducible factor-1 (HIF-1) by the protein 
      arginine methyltransferase PRMT1.
PG  - 925-35
LID - 10.1091/mbc.E13-07-0423 [doi]
AB  - Hypoxia-inducible factors (HIF-1 and HIF-2) are essential mediators for the 
      adaptive transcriptional response of cells and tissues to low-oxygen conditions. 
      Under hypoxia or when cells are treated with various nonhypoxic stimuli, the 
      active HIF-alpha subunits are mainly regulated through increased protein 
      stabilization. For HIF-1alpha, it is clear that further transcriptional, 
      translational, and posttranslational regulations are important for complete HIF-1 
      activity. Novel evidence links hypoxia and HIF-1 to arginine methylation, an 
      important protein modification. These studies suggest that arginine 
      methyltransferases may be important for hypoxic responses. Protein arginine 
      methyltransferase 1 (PRMT1), the predominant arginine methyltransferase, can act 
      as a transcriptional activator or repressor by modifying a diverse set of 
      substrates. In this work, we show that PRMT1 is a repressor of both HIF-1 and 
      HIF-2. The cellular depletion of PRMT1 by small interference RNA targeting leads 
      to increased HIF transcriptional activity. This activation is the result of 
      enhanced HIF-alpha subunit transcription, which allows increased HIF-alpha subunit 
      availability. We provide evidence that PRMT1-dependent HIF-1alpha regulation is 
      mediated through the activities of both specificity protein 1 (Sp1) and Sp3, two 
      transcription factors known to control HIF-1alpha expression. This study therefore 
      identifies PRMT1 as a novel regulator of HIF-1- and HIF-2-mediated responses.
FAU - Lafleur, Veronique N
AU  - Lafleur VN
AD  - Centre de Recherche du CHU de Quebec, L'Hotel-Dieu de Quebec, and Department of 
      Molecular Biology, Medical Biochemistry and Pathology, Universite Laval, Quebec, 
      QC G1R 2J6, Canada Lady Davis Institute for Medical Research, Sir Mortimer B. 
      Davis Jewish General Hospital, and Departments of Oncology and Medicine, McGill 
      University, Montreal, QC H3G 1Y6, Canada.
FAU - Richard, Stephane
AU  - Richard S
FAU - Richard, Darren E
AU  - Richard DE
LA  - eng
GR  - MOP-102760/Canadian Institutes of Health Research/Canada
GR  - MOP-93811/Canadian Institutes of Health Research/Canada
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140122
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Basic Helix-Loop-Helix Transcription Factors)
RN  - 0 (HIF1A protein, human)
RN  - 0 (Hypoxia-Inducible Factor 1, alpha Subunit)
RN  - 0 (RNA, Small Interfering)
RN  - 0 (Repressor Proteins)
RN  - 0 (SP3 protein, human)
RN  - 0 (Sp1 Transcription Factor)
RN  - 148710-94-5 (Sp3 Transcription Factor)
RN  - 1B37H0967P (endothelial PAS domain-containing protein 1)
RN  - 94ZLA3W45F (Arginine)
RN  - EC 1.13.12.- (Luciferases)
RN  - EC 2.1.1.319 (PRMT1 protein, human)
RN  - EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
SB  - IM
MH  - Arginine/metabolism
MH  - Basic Helix-Loop-Helix Transcription Factors/genetics/*metabolism
MH  - Cell Hypoxia/genetics
MH  - *Gene Expression Regulation
MH  - Genes, Reporter
MH  - HEK293 Cells
MH  - HeLa Cells
MH  - Humans
MH  - Hypoxia-Inducible Factor 1, alpha Subunit/genetics/*metabolism
MH  - Luciferases/genetics/metabolism
MH  - Methylation
MH  - *Protein Processing, Post-Translational
MH  - Protein-Arginine N-Methyltransferases/antagonists & 
      inhibitors/genetics/*metabolism
MH  - RNA, Small Interfering/genetics/metabolism
MH  - Repressor Proteins/antagonists & inhibitors/genetics/*metabolism
MH  - Signal Transduction
MH  - Sp1 Transcription Factor/genetics/metabolism
MH  - Sp3 Transcription Factor/genetics/metabolism
MH  - *Transcription, Genetic
PMC - PMC3952860
EDAT- 2014/01/24 06:00
MHDA- 2014/11/05 06:00
PMCR- 2014/05/30
CRDT- 2014/01/24 06:00
PHST- 2014/01/24 06:00 [entrez]
PHST- 2014/01/24 06:00 [pubmed]
PHST- 2014/11/05 06:00 [medline]
PHST- 2014/05/30 00:00 [pmc-release]
AID - mbc.E13-07-0423 [pii]
AID - E13-07-0423 [pii]
AID - 10.1091/mbc.E13-07-0423 [doi]
PST - ppublish
SO  - Mol Biol Cell. 2014 Mar;25(6):925-35. doi: 10.1091/mbc.E13-07-0423. Epub 2014 Jan 
      22.