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Science 8 April 1994:
Vol. 264. no. 5156, pp. 251 - 254
DOI: 10.1126/science.8146655
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Articles

Science, Vol 264, Issue 5156, 251-254
Copyright © 1994 by American Association for the Advancement of Science

articles

Binding and suppression of the Myc transcriptional activation domain by p107

W Gu, K Bhatia, IT Magrath, CV Dang, and R Dalla-Favera

Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.

An amino-terminal transactivation domain is required for Myc to function as a transcription factor controlling cell proliferation, differentiation, and apoptosis. A complementary DNA expression library was screened with a Myc fusion protein to identify proteins interacting with this domain, and a clone encoding the Rb-related p107 protein was isolated. The p107 protein was shown to associate with Myc in vivo and to suppress the activity of the Myc transactivation domain. However, mutant forms of Myc from Burkitt lymphoma cells, which contain sequence alterations in the transactivation domain, were resistant to p107-mediated suppression. Thus, disruption of a regulatory interaction between Myc and p107 may be important in tumorigenesis.


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