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Mol Cell Biol, April 1998, p. 2230-2239, Vol. 18, No. 4
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Notch Inhibition of E47 Supports the Existence of a Novel Signaling Pathway

Peter Ordentlich,1 Arthur Lin,1 Chun-Pyn Shen,1 Chris Blaumueller,2 Kenji Matsuno,1 Spyros Artavanis-Tsakonas,2 and Tom Kadesch1,*

Howard Hughes Medical Institute and Department of Genetics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6145,1 and Howard Hughes Medical Institute and Departments of Cell Biology and Biology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 065362

Received 12 September 1997/Returned for modification 14 November 1997/Accepted 3 January 1998

E47 is a widely expressed transcription factor that activates B-cell-specific immunoglobulin gene transcription and is required for early B-cell development. In an effort to identify processes that regulate E47, and potentially B-cell development, we found that activated Notch1 and Notch2 effectively inhibit E47 activity. Only the intact E47 protein was inhibited by Notch---fusion proteins containing isolated DNA binding and activation domains were unaffected---suggesting that Notch targets an atypical E47 cofactor. Although overexpression of the coactivator p300 partially reversed E47 inhibition, results of several assays indicated that p300/CBP is not a general target of Notch. Notch inhibition of E47 did not correlate with its ability to activate CBF1/RBP-Jkappa , the mammalian homolog of Suppressor of Hairless, a protein that associates physically with Notch and defines the only known Notch signaling pathway in drosophila. Importantly, E47 was inhibited independently of CBF1/RPB-Jkappa by Deltex, a second Notch-interacting protein. We provide evidence that Notch and Deltex may act on E47 by inhibiting signaling through Ras because (i) full E47 activity was found to be dependent on Ras and (ii) both Notch and Deltex inhibited GAL4-Jun, a hybrid transcription factor whose activity is dependent on signaling from Ras to SAPK/JNK.

* Corresponding author. Mailing address: Howard Hughes Medical Institute and Department of Genetics, University of Pennsylvania School of Medicine, 422 Curie Blvd., Philadelphia, PA 19104-6145. Phone: (215) 898-1047. Fax: (215) 898-9750. E-mail: kadesch{at}mail.med.upenn.edu.




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