Historical Background
Mouse Mdm4 (murine double minute 4) was first identified in an attempt to isolate a novel human p53-binding protein by screening a mouse cDNA library (Shvarts et al. 1996). Subsequently, its human homolog, MDM4, was cloned through a screen that used mouse Mdm4 cDNA as probe (Shvarts et al. 1997). Human MDM4 protein is 90% similar to mouse Mdm4 (Shvarts et al. 1997), with the greatest homology in the N-terminal p53-binding domain, and is ubiquitously expressed in tissues and organs (Shvarts et al. 1996; Shvarts et al. 1997). Importantly, MDM4 is homologous to MDM2, a key E3 ubiquitin ligase that negatively regulates the tumor suppressor p53 (Shvarts et al. 1996) (see also the MDM2 section). Therefore, overexpression of MDM4 leads to the suppression of p53 activity (Shvarts et al. 1996). However, subsequent...
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Acknowledgments
The work in the Kurokawa laboratory is supported by an NCI Career Development Award R00 CA140948 (to M.K.), an American Cancer Society Institutional Research Grant IRG-82-003-30 (to M.K.), a Norris Cotton Cancer Center Prouty grant (to M.K.), and a Norris Cotton Cancer Center Holland Award (to M.K.).
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Huang, A., Yang, E., Kurokawa, M. (2018). MDM4 (Murine Double Minute 4). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101575
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