کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1931493 1050554 2010 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
BAG3 directly associates with guanine nucleotide exchange factor of Rap1, PDZGEF2, and regulates cell adhesion
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
BAG3 directly associates with guanine nucleotide exchange factor of Rap1, PDZGEF2, and regulates cell adhesion
چکیده انگلیسی

BAG3, a member of the Hsc70 binding co-chaperone BAG-family proteins, has critical roles in regulating actin organization, cell adhesion, cell motility and tumor metastasis. The PDZ domain containing guanine nucleotide exchange factor 2 (PDZGEF2) was cloned as a BAG3-interacting protein. PDZGEF2 induces activation of Rap1 and increases integrin-mediated cell adhesion. The PPDY motif at the C-terminus of PDZGEF2 binds to the WW domain of BAG3 in vitro and in vivo. BAG3 deletion mutant lacking the WW domain lose its cell adhesion and motility activity. Gene knockdown of PDZGEF2 leads to the loss of cell adhesion on fibronectin-coated plates while BAG3 overexpression increases cell adhesion in Cos7 cells, but not in PDZGEF2 gene knockdown cells indicating that PDZGEF2 is a critical partner for BAG3 in regulating cell adhesion.

Research highlights
► PDZGEF2 was cloned as a BAG3-interacting protein.
► The PPDY motif of PDZGEF2 binds to the WW domain of BAG3.
► BAG3 deletion WW mutant loses cell adhesion and motility.
► PDZGEF2 is a critical partner of BAG3 for regulating cell adhesion.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 400, Issue 3, 24 September 2010, Pages 413–418
نویسندگان
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