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Science 27 March 1992:
Vol. 255. no. 5052, pp. 1700 - 1702
DOI: 10.1126/science.1372755

Articles

Science, Vol 255, Issue 5052, 1700-1702
Copyright © 1992 by American Association for the Advancement of Science


articles

Inhibition of myeloid differentiation by the helix-loop-helix protein Id

BL Kreider, R Benezra, G Rovera, and T Kadesch

Wistar Institute of Anatomy and Biology, Philadelphia, PA 19104.

Id is a helix-loop-helix (HLH) protein that represses activity of several basic helix-loop-helix (bHLH) proteins involved in cell type--specific transcription and cell lineage commitment. The myeloid precursor cell line 32DC13(G) expressed Id messenger RNA, which was transiently decreased when cells were induced to terminally differentiate with granulocyte--colony-stimulating factor. Concomitant with the decrease of Id messenger RNA was the appearance in nuclear extracts of DNA binding proteins that recognized a canonical E-box motif, a DNA binding site for some bHLH proteins. Constitutive expression of an Id complementary DNA in 32DC13(G) cells blocked their ability to differentiate and to induce E-box-binding activity. These results suggest that Id and, hence, bHLH proteins function in the process of myeloid differentiation.


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L. A. Milner, A. Bigas, R. Kopan, C. Brashem-Stein, I. D. Bernstein, and D. I. K. Martin (1996)
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MIDA1, a Protein Associated with Id, Regulates Cell Growth.
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Inhibition of an Erythroid Differentiation Switch by the Helix-Loop-Helix Protein Id1.
J. Lister, W. C. Forrester, and M. H. Baron (1995)
J. Biol. Chem. 270, 17939-17946
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The Upstream Promoter Element of the Glucagon Gene, G1, Confers Pancreatic Alpha Cell-specific Expression.
C. Morel, M. Cordier-Bussat, and J. Philippe (1995)
J. Biol. Chem. 270, 3046-3055
   Abstract »    Full Text »    PDF »
The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein..
A Iavarone, P Garg, A Lasorella, J Hsu, and M A Israel (1994)
Genes & Dev. 8, 1270-1284
   Abstract »    PDF »
Regulation of lymphoid-specific immunoglobulin mu heavy chain gene enhancer by ETS-domain proteins.
B Nelsen, G Tian, B Erman, J Gregoire, R Maki, B Graves, and R Sen (1993)
Science 261, 82-86
   Abstract »    PDF »
Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins..
Y Jen, H Weintraub, and R Benezra (1992)
Genes & Dev. 6, 1466-1479
   Abstract »    PDF »
Molecular Cloning and Characterization of a Zinc Finger Protein Involved in Id-1-stimulated Mammary Epithelial Cell Growth.
J. Singh, Y. Itahana, S. Parrinello, K. Murata, and P.-Y. Desprez (2001)
J. Biol. Chem. 276, 11852-11858
   Abstract »    Full Text »    PDF »
Regulation of Id2 Gene Expression by the Insulin-like Growth Factor I Receptor Requires Signaling by Phosphatidylinositol 3-Kinase.
B. Belletti, M. Prisco, A. Morrione, B. Valentinis, M. Navarro, and R. Baserga (2001)
J. Biol. Chem. 276, 13867-13874
   Abstract »    Full Text »    PDF »
Commitment to natural killer cells requires the helix-loop-helix inhibitor Id2.
T. Ikawa, S. Fujimoto, H. Kawamoto, Y. Katsura, and Y. Yokota (2001)
PNAS 98, 5164-5169
   Abstract »    Full Text »    PDF »



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