| First Author | Blackwood EM | Year | 1992 |
| Journal | Genes Dev | Volume | 6 |
| Issue | 1 | Pages | 71-80 |
| PubMed ID | 1730411 | Mgi Jnum | J:19398 |
| Mgi Id | MGI:67567 | Doi | 10.1101/gad.6.1.71 |
| Citation | Blackwood EM, et al. (1992) Myc and Max associate in vivo. Genes Dev 6(1):71-80 |
| abstractText | Max is a helix-loop-helix zipper protein that associates in vitro with Myc family proteins to form a sequence-specific DNA-binding complex. We show here, by means of a coimmunoprecipitation assay with anti-Myc and anti-Max antibodies, that Myc and Max are associated in vivo and essentially all of the newly synthesized Myc can be detected in a complex with Max. This complex possesses specific DNA-binding activity for CACGTG-containing oligonucleotides. Although Max itself is a highly stable protein, Myc is rapidly degraded during or after its association with Max. In vivo Max is shown to be a nuclear protein phosphorylated by casein kinase II, and alternatively spliced forms of Max are expressed in cells. Furthermore, the levels of Max expression are equivalent in quiescent, mitogen-stimulated, and cycling cells. We conclude that the highly regulated rate of Myc biosynthesis is likely to be a limiting step in the formation of Myc:Max complexes. |
