PMID- 10597290
OWN - NLM
STAT- MEDLINE
DCOM- 20000106
LR  - 20061115
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 18
IP  - 48
DP  - 1999 Nov 18
TI  - Nmi protein interacts with regions that differ between MycN and Myc and is
      localized in the cytoplasm of neuroblastoma cells in contrast to nuclear MycN.
PG  - 6810-7
AB  - Myc family proteins play an important role in cellular processes such as
      proliferation, differentiation, apoptosis and transformation. A number of
      interaction partners of Myc have been identified, such as Max, p107, TBP, YY1,
      Miz-1, AP-2 and Nmi. Both Max and Nmi also bind to MycN. In contrast to the well 
      defined binding of Max to Myc family proteins the interaction of Nmi with Myc or 
      MycN is only poorly characterized. By employing the yeast two-hybrid system we
      have mapped the regions of MycN and Myc responsible for binding to Nmi. For MycN 
      exclusively a central region mediates binding to Nmi. In contrast, for Myc a
      C-terminal portion of the protein, and possibly also a central part, is involved 
      in Nmi interaction. Nmi does not interact with Max and has no transactivation
      capabilities in yeast, suggesting that Nmi alone is not a transcriptional
      activator in mammalian cells. Immunofluorescence demonstrates that both in 293
      embryonic kidney cells and in Kelly neuroblastoma cells all detectable
      ectopically expressed Nmi is localized in the cytoplasm, in part in a punctate,
      granular pattern. MycN, which is highly expressed in Kelly cells consequent to
      amplification, appears to be localized exclusively in the nuclei. This directly
      demonstrates that in the same cell at least the major proportion of MycN and Nmi 
      is localized in different cellular compartments. This result is confirmed by the 
      finding that endogenous Nmi, which is expressed in Kelly cells only after
      stimulation with interferon gamma, is detected exclusively in the cytoplasm of
      these cells. Therefore only a very small amount of MycN and Nmi is likely to be
      involved in MycN/Nmi interaction in vivo.
FAU - Bannasch, D
AU  - Bannasch D
AD  - Division of Cytogenetics-H0400, Deutsches Krebsforschungszentrum, Heidelberg,
      Germany.
FAU - Weis, I
AU  - Weis I
FAU - Schwab, M
AU  - Schwab M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Carrier Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (NMI protein, human)
RN  - 0 (Proto-Oncogene Proteins c-myc)
SB  - IM
MH  - Carrier Proteins/*metabolism
MH  - Cell Nucleus/*metabolism
MH  - Cytoplasm/*metabolism
MH  - Humans
MH  - *Intracellular Signaling Peptides and Proteins
MH  - Neuroblastoma/*metabolism/pathology
MH  - Protein Binding
MH  - Proto-Oncogene Proteins c-myc/*metabolism
MH  - Tumor Cells, Cultured
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.1203090 [doi]
PST - ppublish
SO  - Oncogene. 1999 Nov 18;18(48):6810-7. doi: 10.1038/sj.onc.1203090.