tailieunhanh - Báo cáo khoa học: SHIP2 interaction with the cytoskeletal protein Vinexin

The src homology 2 (SH2) domain-containing inositol 5-phosphatase 2 (SHIP2) catalyses the dephosphorylation of phosphatidylinositol 3,4,5-tris-phosphate [PtdIns(3,4,5)P3] to phosphatidylinositol 3,4-bisphosphate [PtdIns(3,4)P2]. We report the identification of the cytoskeletal protein Vinexin as a protein interacting with SHIP2. | iFEBS Journal SHIP2 interaction with the cytoskeletal protein Vinexin Nathalie Paternotte1 Jing Zhang1 Isabelle Vandenbroere1 Katrien Backers1 Daniel Blero1 Noriyuki Kioka2 Jean-Marie Vanderwinden3 Isabelle Pirson1 and Christophe Erneux1 1 Interdisciplinary Research Institute IRIBHM Universite Libre de Bruxelles Brussels Belgium 2 Division of Applied Life Sciences Graduate Schoolof Agriculture Kyoto University Japan 3 Laboratoire de Neurophysiologie University Libre de Bruxelles Brussels Belgium Keywords cellular adhesion phosphatidylinositol 3 4 5-trisphosphate SHIP2 signal transduction Vinexin Correspondence C. Erneux Institute of Interdisciplinary Research IRIBHM Campus Erasme Building C 808 Route de Lennik 1070 Brussels Belgium Fax 32 2 555 4655 Tel 32 2 555 4162 E-mail cerneux@ Received 25 August 2005 accepted 28 September 2005 doi The src homology 2 SH2 domain-containing inositol 5-phosphatase 2 SHIP2 catalyses the dephosphorylation of phosphatidylinositol 3 4 5-tris-phosphate PtdIns 3 4 5 P3 to phosphatidylinositol 3 4-bisphosphate PtdIns 3 4 P2 . We report the identification of the cytoskeletal protein Vinexin as a protein interacting with SHIP2. This was achieved by yeast two-hybrid screening using the C-terminal region of SHIP2 as bait. Vinexin has previously been identified as a vinculin-binding protein that plays a key role in cell spreading and cytoskeletal organization. The interaction between SHIP2 and Vinexin was confirmed in lysates of both COS-7 cells and mouse embryonic fibroblasts MEF . The C-terminus was involved in the interaction as shown by the transfection of a truncated C-terminus mutant of SHIP2. In addition we showed the colocalization between Vine-xin a and SHIP2 at the periphery of transfected COS-7 cells. When added in vitro to SHIP2 Vinexin did not affect the PtdIns 3 4 5 P3 5-phosphatase activity of SHIP2. Enhanced cell adhesion to collagen-I-coated dishes was shown upon transfection of .

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