Nuclear translocation of lysyl oxidase is promoted by interaction with transcription repressor p66ß.

Lysyl oxidase (LOX) is an amine oxidase involved in protein cross-linking of the extracellular matrix. Less well characterized is the role that LOX plays among nuclear proteins, and molecular mechanisms of its transport to the nucleus are currently unknown. Here, we have employed yeast two-hybrid library screening and found that the LOX catalytic domain interacts with the transcription repressor p66ß. This interaction has been confirmed in vitro and has been found to be accomplished through the CR2-containing domain of p66ß. Moreover, co-expression of p66ß and LOX in living tumor cells leads to the nuclear accumulation of LOX. Thus, p66ß might be important for the regulation of LOX in the nucleus.