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INTRODUCTION ============ GADD (growth arrest and DNA-damage inducible) 45α is a multi-functional protein implicated in a variety of cellular stress responses ([@gkt223-B1],[@gkt223-B2]). Upregulation of GADD45α expression has been shown to link to the G~2~/M checkpoint of the cell cycle by inhibiting CDC2 kinase activity ([@gkt223-B3]). In addition, GADD45α also functions in modulating genomic DNA demethylation and DNA-damage repair responses, and therefore contributing to the genome stability ([@gkt223-B4],[@gkt223-B5]). Furthermore, induction of GADD45α represents an important cellular mechanism to trigger the apoptosis in responding to various harmful stresses ([@gkt223-B6; @gkt223-B7; @gkt223-B8]). The induction of GADD45α expression can be regulated at multiple steps, including the transcriptional, post-transcriptional, translational and post-translational events, and the mechanisms involved in these processes are also complicated ([@gkt223-B2],[@gkt223-B4],[@gkt223-B7],[@gkt223-B9; @gkt223-B10; @gkt223-B11]). In our previously study, we demonstrated that GADD45α is a liable protein and undergoes constitutive ubiquitination and proteasome-dependent degradation in the resting cells. Arsenite, a toxic chemical agent with anticancer usage, has effects to interrupt endogenous GADD45α ubiquitination and degradation, leading to GADD45α protein accumulation and cellular apoptosis ([@gkt223-B7],[@gkt223-B12]). These findings provide a new model for GADD45α functional regulation through the modulation of its protein stability *in vivo*. However, the factors and mechanisms involved in the cellular GADD45α protein stability regulation are still poorly understood yet. The oncoprotein MDM2 (mouse counterpart of HDM2 in human) is a ring-finger-containing E3 ubiquitin ligase, which is well known as a feedback regulator of the tumor suppressor p53. It binds to and mediates the ubiquitination and degradation of p53, thereby contributing greatly to the cellular p53 functional control. Various damaging stresses can trigger the interruption of constitutive p53--MDM2 interaction, leading to p53 accumulation and fully functional activation to mediate diverse cellular biological effects ([@gkt223-B13]). A lot of regulatory factors have been demonstrated to act on MDM2 and modulate p53 stability and transactivity under various stress conditions ([@gkt223-B14]). The latest players in MDM2--p53 pathway regulation are a subset of ribosomal proteins (RPs) with well-established extraribosomal functions, including the large subunit RPs, L5 ([@gkt223-B15]), L11 ([@gkt223-B16; @gkt223-B17; @gkt223-B18]), L23 ([@gkt223-B19],[@gkt223-B20]), L26 ([@gkt223-B21],[@gkt223-B22]), and the small subunit RPs, S7 ([@gkt223-B23],[@gkt223-B24]) and S3 ([@gkt223-B25]). The binding of these RPs to MDM2 have been reported with effects of blocking the E3 ubiquitin ligase activity of MDM2, thereby contributing to p53 upregulation and functional activation under the ribosomal biogenesis stress conditions ([@gkt223-B26; @gkt223-B27; @gkt223-B28]). Furthermore, each of the ribosomal protein binds to overlapping yet distinct domains within the central region of MDM2. Therefore, the interdependence interaction of the different ribosomal proteins to MDM2 might be critical for regulating the E3 ubiquitin ligase activity of MDM2 by similar but not identical mechanism and indicates the potential and specific roles of these RPs in sensing different types of stress signals ([@gkt223-B15],[@gkt223-B17],[@gkt223-B19],[@gkt223-B23],[@gkt223-B26; @gkt223-B27; @gkt223-B28]). In this study, we show that GADD45α, MDM2 and a small subunit of RPs, S7, interact with each other in human cells. Interaction with MDM2 serves as a mechanism for GADD45α protein undergoing the dynamic ubiquitination and degradation process *in vivo*; although by associating with MDM2, S7 has