Regulation of cell-cycle movement and cell transformation by c-Myc and its binding proteins

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1).MM-1MM-1 was found to have an mutation of alanine (A) at amino acid number 157 to arginine (R) in a high frequency of the patients of leukemia, lymphoma and scc-type of tongue cancers. This mutation of MM-1 abrogates all the functions of MM-1 to c-Myc, including repression of activities for transcription, cell transformation, and cell growth. The transrepression pathway of MM-1 to c-Myc was found to be carried out by the recruitment of HDAC complex by TIF1b that MM-1 binds. Furthermore, we have found that MM-1 also stimulates the degradation of c-Myc in a ubiquitin-independent manner and that this activity of A157R mutation of MM-1 was hampered. We also identified the splicing isoforms of MM-1 by an alternative splicing of the gene mapped to chromosome 12 and each isoform was found to be distinctly located in cells.2).AMY-1AMY-1 was found to bind to WAVE1 to relocalize the site for actin polymerization and also to AKAP84, an anchoring protein of A-kinase, for participating in the spermatogenesis.3). MSSPDisruption of mssp gene in mice showed some embryonic lethality, indication that MSSP functions in early embryogenesis.