PMID- 10597267
OWN - NLM
STAT- MEDLINE
DCOM- 20000106
LR  - 20071114
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 18
IP  - 48
DP  - 1999 Nov 18
TI  - Mmip-2, a novel RING finger protein that interacts with mad members of the Myc
      oncoprotein network.
PG  - 6621-34
AB  - Mad proteins are basic-helix-loop-helix-leucine zipper (bHLH-ZIP)-containing
      members of the myc oncoprotein network. They interact with the bHLH-ZIP protein
      max, compete for the same DNA binding sites as myc-max heterodimers and
      down-regulate myc-responsive genes. Using the bHLH-ZIP domain of mad1 as a yeast 
      two-hybrid 'bait', we identified Mmip-2, a novel RING finger protein that
      interacts with all mad members, but weakly or not at all with c-myc, max or
      unrelated bHLH or bZIP proteins. The mad1-Mmip-2 interaction is mediated by the
      ZIP domain in the former protein and by at least two regions in the latter which 
      do not include the RING finger. Mmip-2 can disrupt max-mad DNA binding and can
      reverse the suppressive effects of mad proteins on c-myc-responsive target genes 
      and on c-myc + ras-mediated focus formation in fibroblasts. Tagging with spectral
      variants of green fluorescent protein showed that Mmip-2 and mad proteins reside 
      in separate cytoplasmic and nuclear compartments, respectively. When
      co-expressed, however, the proteins interact and translocate to the cellular
      compartment occupied by the more abundant protein. These observations suggest a
      novel way by which Mmip-2 can modulate the transcriptional activity of myc
      oncoproteins.
FAU - Yin, X Y
AU  - Yin XY
AD  - Section of Hematology/Oncology, Children's Hospital of Pittsburgh, University of 
      Pittsburgh Cancer Institute, PA 15213, USA.
FAU - Gupta, K
AU  - Gupta K
FAU - Han, W P
AU  - Han WP
FAU - Levitan, E S
AU  - Levitan ES
FAU - Prochownik, E V
AU  - Prochownik EV
LA  - eng
SI  - GENBANK/AF190166
GR  - HL33741/HL/NHLBI NIH HHS/United States
GR  - NS32385/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Fungal Proteins)
RN  - 0 (MAD1 protein, S cerevisiae)
RN  - 0 (MAD1L1 protein, human)
RN  - 0 (Mad1l1 protein, mouse)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proto-Oncogene Proteins c-myc)
RN  - 0 (Repressor Proteins)
RN  - 0 (Rnf17 protein, mouse)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - 3T3 Cells
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - *Carrier Proteins
MH  - Cell Cycle Proteins
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Fungal Proteins/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/*metabolism
MH  - Phosphoproteins/*metabolism
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Proto-Oncogene Proteins c-myc/*metabolism
MH  - *Repressor Proteins
MH  - Saccharomyces cerevisiae/genetics
MH  - Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
MH  - Subcellular Fractions/metabolism
MH  - Transcription Factors/chemistry/genetics/*metabolism
MH  - Two-Hybrid System Techniques
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1038/sj.onc.1203097 [doi]
PST - ppublish
SO  - Oncogene. 1999 Nov 18;18(48):6621-34. doi: 10.1038/sj.onc.1203097.