TAILIEUCHUNG - Báo cáo khoa học: Structural bases for recognition of Anp32⁄LANP proteins

Death-associated protein kinase 1 (DAPK-1) is a multidomain protein kinase with diverse roles in autophagic, apoptotic and survival pathways. Bioinformatic screens were used to identify a small internal mRNA from the DAPK-1locus (named s-DAPK-1). | ễFEBS Journal Structural bases for recognition of Anp32 LANP proteins Cesira de Chiara Rajesh P. Menon and Annalisa Pastore National institute for MedicalResearch The Ridgeway London UK Keywords ataxin 1 leucine-rich repeats NMR PP2A inhibitor structure Correspondence A. Pastore National institute for Medical Research The Ridgeway London NW7 1AA UK Fax 44 208 906 4477 Tel 44 208 959 3666 E-mail apastor@ Received 13 January 2008 revised 3 March 2008 accepted 14 March 2008 doi The leucine-rich repeat acidic nuclear protein Anp32a LANP belongs to a family of evolutionarily-conserved phosphoproteins involved in a complex network of protein-protein interactions. In an effort to understand the cellular role we have investigated the mode of interaction of Anp32a with its partners. As a prerequisite we solved the structure in solution of the evolutionarily conserved N-terminal leucine-rich repeat LRR domain and modeled its interactions with other proteins taking PP2A as a paradigmatic example. The interaction between the Anp32a LRR domain and the AXH domain of ataxin-1 was probed experimentally. The two isolated and unmodified domains bind with very weak millimolar affinity thus suggesting the necessity either for an additional partner . other regions of either or both proteins or a third molecule or for a post-translational modification. Finally we identified by two-hybrid screening a new partner of the LRR domain . the microtubule plus-end tracking protein Clip 170 Restin known to regulate the dynamic properties of microtubules and to be associated with severe human pathologies. The leucine-rich repeat acidic nuclear protein Anp32a LANP is a member of the Anp32 family of acidic nuclear evolutionarily-conserved phosphoproteins which present a broad range of activities 1 . They are characterized by the presence of a highly conserved N-terminal domain containing leucine-rich repeats LRRs motifs known to mediate .

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