PP2A binds the LIM-domains of Lipoma Preferred Partner via its PR130/B” subunit to regulate cell adhesion and migration

نویسندگان

  • Veerle JANSSENS
  • Karen ZWAENEPOEL
  • Carine ROSSÉ
  • Marleen M. R. PETIT
  • Jozef GORIS
  • Peter J. PARKER
چکیده

1 Francis Crick Institute, Protein Phosphorylation Laboratory, 44 Lincoln’s Inn Fields, WC2A 3PX, London, UK 2 Laboratory of Protein Phosphorylation and Proteomics, Dept. of Cellular and Molecular Medicine, KU Leuven, Herestraat 49 PO-box 901, B-3000 Leuven, Belgium 3 Research Centre, Institut Curie, 75005 Paris, France 4 Molecular Oncology Laboratory, Dept. of Human Genetics, KU Leuven, Herestraat 49 PObox 602, B-3000 Leuven, Belgium 5 Division of Cancer Studies King’s College London, Guy’s Hospital Campus, Thomas Street, London SE1 9RT, UK.

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PP2A binds to the LIM domains of lipoma-preferred partner through its PR130/B″ subunit to regulate cell adhesion and migration.

Here, we identify the LIM protein lipoma-preferred partner (LPP) as a binding partner of a specific protein phosphatase 2A (PP2A) heterotrimer that is characterised by the regulatory PR130/B″α1 subunit (encoded by PPP2R3A). The PR130 subunit interacts with the LIM domains of LPP through a conserved Zn²⁺-finger-like motif in the differentially spliced N-terminus of PR130. Isolated LPP-associated...

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تاریخ انتشار 2016