Max-interacting transcriptional repressor MAD4 is a
protein that in humans is encoded by the MXD4gene.[5][6]
Function
This gene is a member of the
MAD gene family . The MAD genes encode basic helix-loop-helix-
leucine zipper proteins that heterodimerize with
MAX protein, forming a
transcriptional repression complex. The MAD proteins compete for MAX binding with MYC, which
heterodimerizes with MAX forming a transcriptional activation complex. Studies in rodents suggest that the MAD genes are tumor suppressors and contribute to the regulation of cell growth in differentiating tissues.[6]
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8.
Bibcode:
2005Natur.437.1173R.
doi:
10.1038/nature04209.
PMID16189514.
S2CID4427026.
Marcotte R, Chen JM, Huard S, Wang E (December 2005). "c-Myc creates an activation loop by transcriptionally repressing its own functional inhibitor, hMad4, in young fibroblasts, a loop lost in replicatively senescent fibroblasts". Journal of Cellular Biochemistry. 96 (5): 1071–85.
doi:
10.1002/jcb.20503.
PMID16167342.
S2CID8251961.
Pope SN, Lee IR (February 2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". The Journal of Steroid Biochemistry and Molecular Biology. 94 (1–3): 203–8.
doi:
10.1016/j.jsbmb.2005.01.007.
PMID15862967.
S2CID9746088.
Max-interacting transcriptional repressor MAD4 is a
protein that in humans is encoded by the MXD4gene.[5][6]
Function
This gene is a member of the
MAD gene family . The MAD genes encode basic helix-loop-helix-
leucine zipper proteins that heterodimerize with
MAX protein, forming a
transcriptional repression complex. The MAD proteins compete for MAX binding with MYC, which
heterodimerizes with MAX forming a transcriptional activation complex. Studies in rodents suggest that the MAD genes are tumor suppressors and contribute to the regulation of cell growth in differentiating tissues.[6]
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8.
Bibcode:
2005Natur.437.1173R.
doi:
10.1038/nature04209.
PMID16189514.
S2CID4427026.
Marcotte R, Chen JM, Huard S, Wang E (December 2005). "c-Myc creates an activation loop by transcriptionally repressing its own functional inhibitor, hMad4, in young fibroblasts, a loop lost in replicatively senescent fibroblasts". Journal of Cellular Biochemistry. 96 (5): 1071–85.
doi:
10.1002/jcb.20503.
PMID16167342.
S2CID8251961.
Pope SN, Lee IR (February 2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". The Journal of Steroid Biochemistry and Molecular Biology. 94 (1–3): 203–8.
doi:
10.1016/j.jsbmb.2005.01.007.
PMID15862967.
S2CID9746088.
