High impact information on MXD4

• Using a rat embryo fibroblast transformation assay, we show that both Mad3 and Mad4 inhibit c-Myc dependent cell transformation [1].
• Mad3 and Mad4 interact with both Max and mSin3 and repress transcription from a promoter containing CACGTG binding sites [1].
• The cytoplasmic localization of Mad4 was determined by a CRM1-dependent nuclear export signal located near the amino terminus [2].
• Furthermore, our data derived from competition experiments suggested that the Mad3/Max and Mad4/Max complexes also possess comparable DNA binding affinities [3].
• The isolates included an oncogenic variant (MAD-4), an antigenic variant (MAD-11), and two different isolates derived from the urine (MAD-7) and from the brain (MAD-8) of the same patient [4].

Biological context of MXD4

• Using reporter gene assays in stably transfected MEL cells, we show that induction of Mad4 is mediated by a 49 nt core promoter region [5].
• Mad4 was induced when cells exit the cell cycle and, together with mad1, during the late phase of differentiation [6].

Physical interactions of MXD4

• Human liver specific transcriptional factor TCP10L binds to MAD4 [7].

References