Journal article

Structural basis of the interaction of the breast cancer Oncogene LMO4 with the tumour suppressor CtIP/RBBP8

PH Stokes, CW Liew, AH Kwan, P Foo, HE Barker, A Djamirze, V O'Reilly, JE Visvader, JP Mackay, JM Matthews

Journal of Molecular Biology | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2013

Abstract

LIM-only protein 4 (LMO4) is strongly linked to the progression of breast cancer. Although the mechanisms underlying this phenomenon are not well understood, a role is emerging for LMO4 in regulation of the cell cycle. We determined the solution structure of LMO4 in complex with CtIP (C-terminal binding protein interacting protein)/RBBP8, a tumour suppressor protein that is involved in cell cycle progression, DNA repair and transcriptional regulation. Our data reveal that CtIP and the essential LMO cofactor LDB1 (LIM-domain binding protein 1) bind to the same face on LMO4 and cannot simultaneously bind to LMO4. We hypothesise that overexpression of LMO4 may disrupt some of the normal tumour ..

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University of Melbourne Researchers

Grants

Funding Acknowledgements

P.S. and H.B. were supported by Australian Postgraduate Awards. J.M.M., J.P.M. and J.V. were supported by Senior Research Fellowships and an Australia Fellowship (to J.V.) from the Australian National Health and Medical Research Council. This work was supported by grants from the Australian National Health and Medical Research Council and the Australian Research Council.