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Nuclear translocation of lysyl oxidase is promoted by interaction with transcription repressor p66β

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Abstract

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 p66β. This interaction has been confirmed in vitro and has been found to be accomplished through the CR2-containing domain of p66β. Moreover, co-expression of p66β and LOX in living tumor cells leads to the nuclear accumulation of LOX. Thus, p66β might be important for the regulation of LOX in the nucleus.

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Abbreviations

ECM:

Extracellular matrix

EMT:

Epithelial to mesenchymal transition

LOX:

Lysyl oxidase

ppLOX:

Preprolysyl oxidase

PBS:

Phosphate-buffered saline

TBST:

TRIS-buffered saline with 0.1 % Tween-20

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Acknowledgments

We are grateful to A. Giaccia for anti-LOX antibodies, to H. Nishina, R. Dmitriev, and C. Cardoso for marker plasmids, and to V. Baklaushev for help with confocal microsopy.

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Correspondence to Nikolay B. Pestov.

Additional information

These studies were supported by MCB RAS and the Russian Foundation for Basic Research (grants 13-04-01413 and 12-04-31374).

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Okkelman, I.A., Sukaeva, A.Z., Kirukhina, E.V. et al. Nuclear translocation of lysyl oxidase is promoted by interaction with transcription repressor p66β. Cell Tissue Res 358, 481–489 (2014). https://doi.org/10.1007/s00441-014-1972-z

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  • DOI: https://doi.org/10.1007/s00441-014-1972-z

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