PMID- 10593926
OWN - NLM
STAT- MEDLINE
DCOM- 20000127
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 51
DP  - 1999 Dec 17
TI  - Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of
      transcription factors.
PG  - 36344-50
AB  - Mad:Max heterodimers oppose the growth-promoting action of Myc:Max heterodimers
      by recruiting the mSin3-histone deacetylase (mSin3. HDAC) complex to DNA and
      functioning as potent transcriptional repressors. There are four known members of
      the Mad family that are indistinguishable in their abilities to interact with
      Max, bind DNA, repress transcription, and block Myc + Ras co-transformation. To
      investigate functional differences between Mad family proteins, we have
      identified additional proteins that interact with this family. Here we present
      the identification and characterization of the novel basic-helix-loop-helix
      zipper protein Mlx (Max-like protein x), which is structurally and functionally
      related to Max. The similarities between Mlx and Max include 1) broad expression 
      in many tissues, 2) long protein half-life, and 3) formation of heterodimers with
      Mad family proteins that are capable of specific CACGTG binding. We show that
      transcriptional repression by Mad1:Mlx heterodimers is dependent on dimerization,
      DNA binding, and recruitment of the mSin3A.HDAC corepressor complex. In contrast 
      with Max, Mlx interacts only with Mad1 and Mad4. Together, these findings suggest
      that Mlx may act to diversify Mad family function by its restricted association
      with a subset of the Mad family of transcriptional repressors.
FAU - Billin, A N
AU  - Billin AN
AD  - Huntsman Cancer Institute at the University of Utah, Salt Lake City, Utah
      84112-5550, USA.
FAU - Eilers, A L
AU  - Eilers AL
FAU - Queva, C
AU  - Queva C
FAU - Ayer, D E
AU  - Ayer DE
LA  - eng
SI  - GENBANK/AF203978
GR  - R01 GM055668/GM/NIGMS NIH HHS/United States
GR  - 3P30CA42014/CA/NCI NIH HHS/United States
GR  - GM5568-01/GM/NIGMS 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  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors)
RN  - 0 (Basic-Leucine Zipper Transcription Factors)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (MAX protein, human)
RN  - 0 (MLX protein, human)
RN  - 0 (Myc associated factor X)
RN  - 0 (Tcfl4 protein, mouse)
RN  - 0 (Transcription Factors)
RN  - 137468-70-3 (Max protein, mouse)
SB  - IM
MH  - 3T3 Cells
MH  - Amino Acid Sequence
MH  - Animals
MH  - Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
MH  - Basic-Leucine Zipper Transcription Factors
MH  - Cloning, Molecular
MH  - DNA-Binding Proteins/*genetics/*metabolism
MH  - HeLa Cells
MH  - Helix-Loop-Helix Motifs
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - Transcription Factors/*genetics/*metabolism
MH  - Transcriptional Activation
EDAT- 1999/12/14 00:00
MHDA- 1999/12/14 00:01
CRDT- 1999/12/14 00:00
PHST- 1999/12/14 00:00 [pubmed]
PHST- 1999/12/14 00:01 [medline]
PHST- 1999/12/14 00:00 [entrez]
AID - 10.1074/jbc.274.51.36344 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 17;274(51):36344-50. doi: 10.1074/jbc.274.51.36344.