PMID- 10487760
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20161019
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 18
DP  - 1999 Sep 15
TI  - MEF-2 function is modified by a novel co-repressor, MITR.
PG  - 5085-98
AB  - The MEF-2 proteins are a family of transcriptional activators that have been
      detected in a wide variety of cell types. In skeletal muscle cells, MEF-2
      proteins interact with members of the MyoD family of transcriptional activators
      to synergistically activate gene expression. Similar interactions with tissue or 
      lineage-specific cofactors may also underlie MEF-2 function in other cell types. 
      In order to screen for such cofactors, we have used a transcriptionally inactive 
      mutant of Xenopus MEF2D in a yeast two-hybrid screen. This approach has
      identified a novel protein expressed in the early embryo that binds to XMEF2D and
      XMEF2A. The MEF-2 interacting transcription repressor (MITR) protein binds to the
      N-terminal MADS/MEF-2 region of the MEF-2 proteins but does not bind to the
      related Xenopus MADS protein serum response factor. In the early embryo, MITR
      expression commences at the neurula stage within the mature somites and is
      subsequently restricted to the myotomal muscle. In functional assays, MITR
      negatively regulates MEF-2-dependent transcription and we show that this
      repression is mediated by direct binding of MITR to the histone deacetylase
      HDAC1. Thus, we propose that MITR acts as a co-repressor, recruiting a specific
      deacetylase to downregulate MEF-2 activity.
FAU - Sparrow, D B
AU  - Sparrow DB
AD  - Division of Developmental Biology, National Institute for Medical Research, The
      Ridgeway, Mill Hill, London NW7 1AA.
FAU - Miska, E A
AU  - Miska EA
FAU - Langley, E
AU  - Langley E
FAU - Reynaud-Deonauth, S
AU  - Reynaud-Deonauth S
FAU - Kotecha, S
AU  - Kotecha S
FAU - Towers, N
AU  - Towers N
FAU - Spohr, G
AU  - Spohr G
FAU - Kouzarides, T
AU  - Kouzarides T
FAU - Mohun, T J
AU  - Mohun TJ
LA  - eng
SI  - GENBANK/Z97214
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (MADS Domain Proteins)
RN  - 0 (MEF2 Transcription Factors)
RN  - 0 (MEF2D protein, human)
RN  - 0 (Myogenic Regulatory Factors)
RN  - 0 (Repressor Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (Xenopus Proteins)
RN  - EC 3.5.1.98 (HDAC9 protein, human)
RN  - EC 3.5.1.98 (Histone Deacetylases)
RN  - EC 3.5.1.98 (hdac9-A protein, Xenopus)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Carrier Proteins/genetics/*metabolism
MH  - DNA, Complementary/genetics/isolation & purification
MH  - DNA-Binding Proteins/genetics/*metabolism
MH  - Female
MH  - Gene Expression
MH  - Histone Deacetylases/genetics/metabolism
MH  - Humans
MH  - In Situ Hybridization
MH  - In Vitro Techniques
MH  - MADS Domain Proteins
MH  - MEF2 Transcription Factors
MH  - Molecular Sequence Data
MH  - Muscle, Skeletal/embryology/metabolism
MH  - Mutation
MH  - Myogenic Regulatory Factors
MH  - Repressor Proteins/genetics/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Transcription Factors/genetics/*metabolism
MH  - Transcriptional Activation
MH  - Two-Hybrid System Techniques
MH  - Xenopus/embryology/genetics
MH  - *Xenopus Proteins
PMC - PMC1171579
EDAT- 1999/09/16 00:00
MHDA- 1999/09/16 00:01
CRDT- 1999/09/16 00:00
PHST- 1999/09/16 00:00 [pubmed]
PHST- 1999/09/16 00:01 [medline]
PHST- 1999/09/16 00:00 [entrez]
AID - 10.1093/emboj/18.18.5085 [doi]
PST - ppublish
SO  - EMBO J. 1999 Sep 15;18(18):5085-98. doi: 10.1093/emboj/18.18.5085.