Anne-Sophie Bach, Danielle Derocq, Valérie Laurent-Matha, Philippe Montcourrier, Salwa Sebti, Béatrice Orsetti, Charles Theillet, Céline Gongora, Sophie Pattingre, Eva Ibing, Pascal Roger, Laetitia K Linares, Thomas Reinheckel, Guillaume Meurice, Frank J Kaiser, Christian Gespach, Emmanuelle Liaudet-Coopman
The lysosomal protease cathepsin D (Cath-D) is overproduced in breast cancer cells (BCC) and supports tumor growth and metastasis formation. Here, we describe the mechanism whereby Cath-D is accumulated in the nucleus of ERα-positive (ER+) BCC. We identified TRPS1 (tricho-rhino-phalangeal-syndrome 1), a repressor of GATA-mediated transcription, and BAT3 (Scythe/BAG6), a nucleo-cytoplasmic shuttling chaperone protein, as new Cath-D-interacting nuclear proteins. Cath-D binds to BAT3 in ER+ BCC and they partially co-localize at the surface of lysosomes and in the nucleus...
September 29, 2015: Oncotarget