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J. Biol. Chem., Vol. 277, Issue 11, 9118-9126, March 15, 2002
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From the Department of Laboratory Medicine, Division of Molecular
Medicine, Lund University, University Hospital MAS,
S-205 02 Malmö, Sweden
It is assumed that the Id helix-loop-helix (HLH)
proteins act by associating with ubiquitously expressed basic HLH
(bHLH) transcription factors, such as E47 and E2-2, which prevents
these factors from forming functional hetero- or homodimeric DNA
binding complexes. Several tissue-specific bHLH proteins, including
HASH-1, dHAND, and HES-1, are important for development of the nervous system. Neuroblastoma tumors are derived from the sympathetic nervous
system and exhibit neural crest features. In differentiating neuroblastoma cells, HASH-1 is down-regulated, and there is
coincident up-regulation of the transcriptional repressor HES-1, which
is known to bind the HASH-1 promoter. We found that the
three Id proteins expressed in neuroblastoma cells (Id1, Id2, and Id3) were down-regulated during induced differentiation, indicating that Id
proteins help keep the tumor cells in an undifferentiated state.
Studying interactions, we noted that all four Id proteins could
dimerize with E47 or E2-2, but not with HASH-1 or dHAND. However, the
Id proteins did complex with HES-1, and increased levels of Id2 reduced
the DNA binding activity of HES-1. Furthermore, HES-1 interfered with
Id2/E2-2 complex formation. The ability of Id proteins to affect HES-1
activity is of particular interest in neuronal cells, where regulation
of HES-1 is essential for the timing of neuronal differentiation.
Modulation of Basic Helix-Loop-Helix Transcription Complex
Formation by Id Proteins during Neuronal Differentiation*
,,
*
This work was supported by grants from the Swedish Cancer
Society, the Children's Cancer Foundation of Sweden, Inga and John Hain's Foundation, Åke Wiberg's Foundation, the Crafoord Foundation, HKH Kronprinsessans Lovisas förening för
barnasjukvård, Hans von Kantzow's Foundation, and
Malmö University Hospital Research Funds.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to this work.
§
Present address: Dept. of Medical Biochemistry and Microbiology,
Uppsala University, BMC, P.O. Box 582, S-751 23 Uppsala, Sweden.
¶
To whom correspondence should be addressed: Dept. of
Laboratory Medicine, Div. of Molecular Medicine, Lund University,
University Hospital MAS, Entrance 78, S-205 02 Malmö, Sweden.
Tel.: 46-40337621; Fax: 46-40337322; E-mail:
hakan.axelson@molmed.mas.lu.se.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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