PMID- 10620510
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20181113
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 345 Pt 2
DP  - 2000 Jan 15
TI  - The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) forms a 
      co-repressor complex with mammalian sin3B.
PG  - 335-43
AB  - Winged-helix/forkhead proteins regulate developmental events in both invertebrate
      and vertebrate organisms, but biochemical functions that establish a mechanism of
      action have been defined for only a few members of this extensive gene family.
      Here we demonstrate that MNF (myocyte nuclear factor)-beta, a winged-helix
      protein expressed selectively and transiently in myogenic precursor cells of the 
      heart and skeletal muscles, collaborates with proteins of the mammalian Sin3
      (mSin3) family to repress transcription. Mutated forms of MNF-beta that fail to
      bind mSin3 are defective in transcriptional repression and in negative growth
      regulation, an overexpression phenotype revealed in oncogenic transformation
      assays. These data extend the known repertoire of transcription factors with
      which mSin3 proteins can function as co-repressors to include members of the
      winged-helix gene family. Transcriptional repression by MNF-beta-mSin3 complexes 
      may contribute to the co-ordination of cellular proliferation and terminal
      differentiation of myogenic precursor cells.
FAU - Yang, Q
AU  - Yang Q
AD  - Department of Internal Medicine, University of Texas Southwestern Medical Center,
      5323 Harry Hines Blvd., NB11.200, Dallas, TX 75390-8573, USA.
FAU - Kong, Y
AU  - Kong Y
FAU - Rothermel, B
AU  - Rothermel B
FAU - Garry, D J
AU  - Garry DJ
FAU - Bassel-Duby, R
AU  - Bassel-Duby R
FAU - Williams, R S
AU  - Williams RS
LA  - eng
SI  - GENBANK/AF038848
GR  - HL03231/HL/NHLBI NIH HHS/United States
GR  - HL06296/HL/NHLBI NIH HHS/United States
GR  - HL07360/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Adenovirus E1A Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Forkhead Transcription Factors)
RN  - 0 (Foxk1 protein, mouse)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Protein Isoforms)
RN  - 0 (Proto-Oncogene Proteins c-myc)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (Sin3b protein, mouse)
RN  - 0 (Transcription Factors)
RN  - EC 3.6.5.2 (ras Proteins)
SB  - IM
MH  - Adenovirus E1A Proteins
MH  - Animals
MH  - Binding Sites
MH  - Cell Differentiation
MH  - Cell Transformation, Neoplastic
MH  - DNA-Binding Proteins/*metabolism
MH  - Forkhead Transcription Factors
MH  - Genes, Tumor Suppressor
MH  - *Helix-Loop-Helix Motifs
MH  - Mice
MH  - Molecular Sequence Data
MH  - Muscle, Skeletal/metabolism
MH  - Muscles/cytology
MH  - Myocardium/metabolism
MH  - Nuclear Proteins/*metabolism
MH  - Peptide Fragments/genetics/metabolism
MH  - Protein Binding
MH  - Protein Isoforms
MH  - Proto-Oncogene Proteins c-myc
MH  - Recombinant Proteins/metabolism
MH  - Repressor Proteins/genetics/*metabolism
MH  - Transcription Factors/*metabolism
MH  - Two-Hybrid System Techniques
MH  - ras Proteins
PMC - PMC1220762
EDAT- 2000/01/06 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/01/06 09:00
PHST- 2000/01/06 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/01/06 09:00 [entrez]
PST - ppublish
SO  - Biochem J. 2000 Jan 15;345 Pt 2:335-43.