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The novel protein Memo ( M ediator of  E rbB2 driven cell  mo tility) was identified in a screen for ErbB2 interacting proteins and found to have an essential function in cell motility. Memo is evolutionarily conserved with homologs found in all branches of life; the human and yeast proteins have a similarity of >50%. In the present study we used the model organism  S. cerevisiae  to characterize the Memo-homologue Mho1 (Yjr008wp) and to investigate its function in yeast. In a synthetic lethal screen we found  MHO1  as a novel synthetic lethal partner of  PLC1,  which encodes the single phospholipase C in yeast. Double-deleted cells lacking  MHO1  and  PLC1,  proliferate for up to ten generations. Introduction of human Memo into the  memoΔplc1Δ  strain rescued the synthetic lethal phenotype suggesting that yeast and human proteins have similar functions. Mho1 is present in the cytoplasm and the nucleus of yeast cells; the same distribution of Memo was found in mammalian cells. None of the Memo homologues have a characteristic nuclear localization sequence, however, a conserved nuclear export sequence is found in all. In mammalian cells, blocking nuclear export with Leptomycin B led to nuclear Memo accumulation, suggesting that it is actively exported from the nucleus. In yeast  MHO1  expression is induced by stress conditions. Since invasive growth in  S. cerevisiea  is also stress-induced, we tested Mho1's role in this response.  MHO1  deletion had no effect on invasion induced by nutrient deprivation, however, Mho1 overexpression blocked the invasive ability of yeast cells, suggesting that Mho1 might be acting in a dominant negative manner. Taken together, our results show that  MHO1  is a novel synthetic lethal interactor with  PLC1 , and that both gene products are required for proliferation. Moreover, a role for Memo in cell motility/invasion appears to be conserved across species.

MHO1, an Evolutionarily Conserved Gene, Is Synthetic Lethal with PLC1; Mho1p Has a Role in Invasive Growth