An amino-terminal domain of Mxi1 mediates anti-myc oncogenic activity and interacts with a homolog of the Yeast Transcriptional Repressor SIN3

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• 作者：Nicole Schreiber-Agus ; Lynda Chin ; Ken Chen ; Richard Torres ; Govinda Rao ; Peter Guida ; Arthur I. Skoultchi ; Ronald A. DePinho
• 刊名：Cell
• 出版年：1995
• 出版时间：10 March 1995
• 年：1995
• 卷：80
• 期：5
• 页码：777-786
• 全文大小：1373 K

文摘

Documented interactions among members of the Myc superfamily support a yin-yang model for the regulation of Myc-responsive genes in which transactivation-competent Myc-Max heterodimers are opposed by repressive Mxi1-Max or Mad-Max complexes. Analysis of mouse mxi1 has led to the identification of two mxi1 transcript forms possessing open reading frames that differ in their capacity to encode a short amino-terminal α-helical domain. The presence of this segment dramatically augments the suppressive potential of Mxil and allows for association with a mammalian protein that is structurally homologous to the yeast transcriptional repressor SIN3. These findings provide a mechanistic basis for the antagonistic actions of Mxi1 on Myc activity that appears to be mediated in part through the recruitment of a putative transcriptional repressor.