
The adhesion-regulating molecule 1 (ADRM1) is thought to be involved in protein recruitment and cell adhesion and functions as a proteasomal ubiquitin receptor (1). ADRM1 promotes the activity of UCH-L5 and plays a role in lymphocyte homing. The carboxy-terminal domain of mammalian ADRM1 serves to bind and enhance the isopeptidase activity of UCHL5/UCH37, perhaps serving as a mechanism to accelerate ubiquitin chain disassembly (2,3). ADRM1 expression is induced by IFN-gamma in some cancer cell lines and its expression is upregulated in other metastatic cells, suggesting a role in carcinogenesis (4,5).
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