BAG3 directly associates with guanine nucleotide exchange factor of Rap1, PDZGEF2, and regulates cell adhesion |
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Authors: | Masahiro Iwasaki Ryoichi Tanaka Akinori Hishiya John C Reed |
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Institution: | a The Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA b Medical College of Georgia, 1210 Laney Walker Street, Augusta 92023, GA, USA c The Burnham Institute for Medical Research, La Jolla, CA, USA |
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Abstract: | 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. |
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Keywords: | BAG Bcl-2-associated athanogene PDZGEF2 PDZ domain containing guanine nucleotide exchange factor 2 |
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