کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10816997 | 1058623 | 2008 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
ABLSHIP2DLKMKK7MLK3PKBJIP1SRCTNFGSTJnkPI3KBtk - BTKc-Jun N-terminal kinase - C-Jun N-terminal kinaseMAPK - MAPKPtdIns(3,4,5)P3 - PtdIns (3،4،5) P3PtdIns(4,5)P2 - PtdIns (4،5) P2tumor necrosis factor - فاکتور نکروز تومورphosphatidylinositol 3,4,5-triphosphate - فسفاتیدیلینواستول 3،4،5-تری فسفاتphosphatidylinositol 4,5-bisphosphate - فسفاتیدیلینوزیتول 4،5-بیسفسفاتphosphoinositide 3-kinase - فسفینوزیتید 3-کینازhemagglutinin - هماگلوتینینmitogen-activated protein kinase - پروتئین کیناز فعال با mitogenglutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
SHIP2 (SH2-containing inositol polyphosphate 5-phosphatase 2) is an ubiquitously expressed phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3) 5-phosphatase which contains various motifs susceptible to mediate protein-protein interaction. In cell models, evidence has been provided that SHIP2 plays a role in insulin and growth factor signaling, cytoskeletal organization, cell adhesion and migration. Herein we describe the c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1) as a new protein partner of SHIP2. The interaction between SHIP2 and JIP1 was confirmed in both overexpression systems and native cells. Without modifying the association of JIP1 with the MAPKs in the scaffold complex and with no apparent change of Akt phosphorylation, SHIP2 positively modulated the MLK3/JIP1-mediated JNK1 activation. Moreover, SHIP2 positively regulated the tyrosine phosphorylation of JIP1. This up-regulation was prevented by inhibitors of the Src family and Abl kinases, PP2 and Glivec. The effects of SHIP2 on JNK activity and JIP1 tyrosine phosphorylation were independent of the SHIP2 phosphoinositide 5-phosphatase activity, as similar results were obtained when using a SHIP2 catalytic inactive mutant instead of wild-type SHIP2. Together, these data suggest that by its docking properties, SHIP2 can modulate JIP1-mediated JNK pathway signaling.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 20, Issue 8, August 2008, Pages 1432-1441
Journal: Cellular Signalling - Volume 20, Issue 8, August 2008, Pages 1432-1441
نویسندگان
Jingwei Xie, Sheela Onnockx, Isabelle Vandenbroere, Chantal Degraef, Christophe Erneux, Isabelle Pirson,