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| MAD - A HETERODIMERIC PARTNER FOR MAX THAT ANTAGONIZES MYC TRANSCRIPTIONAL ACTIVITY |
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| Author(s): AYER DE, KRETZNER L, EISENMAN RN |
| Source: CELL Volume: 72 Issue: 2 Pages: 211-222 Published: JAN 29 1993 |
| Times Cited: 569 References: 52 |
| Abstract: Myc family proteins appear to function through heterodimerization with the stable, constitutively expressed bHLH-Zip protein, Max. To determine whether Max mediates the function of regulatory proteins other than Myc, we screened a lambdagt11 expression library with radiolabeled Max protein. One cDNA identified encodes a new member of the bHLH-Zip protein family, Mad. Human Mad protein homodimerizes poorly but binds Max in vitro, forming a sequence-specific DNA binding complex with properties very similar to those of Myc-Max. Both Myc-Max and Mad-Max heterocomplexes are favored over Max homodimers, and, unlike Max homodimers, the DNA binding activity of the heterodimers is unaffected by CKII phosphorylation. Mad does not associate with Myc or with representative bHLH, bZip, or bHLH-Zip proteins. In vivo transactivation assays suggest that Myc-Max and Mad-Max complexes have opposing functions in transcription and that Max plays a central role in this network of transcription factors. |
| Document Type: Article |
| Language: English |
| Reprint Address: AYER, DE (reprint author), FRED HUTCHINSON CANC RES CTR, DEPT BASIC SCI, SEATTLE, WA 98104 USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: KK038 |
| ISSN: 0092-8674 |
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