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Cited by 291

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A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation.

Open access
Ayer, D E, Eisenman, R N·1993·Genes & Development

Abstract

Mad is a basic-helix-loop-helix-zipper protein that heterodimerizes with Max in vitro. Mad:Max heterodimers recognize the same E-box-related DNA-binding sites as Myc:Max heterodimers. However, in transient transfection assays Myc and Mad influence transcription in opposite ways through interaction with Max; Myc activates while Mad represses transcription. Here, we demonstrate that Mad protein is induced rapidly upon differentiation of cells of the myeloid lineage. The Mad protein is synthesized in human cells as a 35-kD nuclear phosphoprotein with an extremely short half-life (t1/2 = 15-30 min) and can be detected in vivo in a complex with Max. In the undifferentiated U937 monocyte cell line Max was found complexed with Myc but not Mad. However, Mad:Max complexes began to accumulate as early as 2 hr after induction of macrophage differentiation with TPA. By 48 hr following TPA treatment only Mad:Max complexes were detectable. These data show that differentiation is accompanied by a change in the composition of Max heterocomplexes. We speculate that this switch in heterocomplexes results in a change in the transcriptional regulation of Myc:Max target genes required for cell proliferation.

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Metadata

Authors
Ayer, D. E., & Eisenman, R. N.
Venue
Genes & Development
Published
1993-11
Volume
7
Issue
11
Pages
2110-2119
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2086132387
Cited by
291
References
1
Type
posted content
Language
en
Open access
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CoChat. (2026). Citation check: A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation. https://app.cochat.ai/papers/10.1101/gad.7.11.2110
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Ayer, D. E., & Eisenman, R. N. (1993). A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation. Genes & Development. https://doi.org/10.1101/gad.7.11.2110

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