BAG3 directly associates with guanine nucleotide exchange factor of Rap1, PDZGEF2, and regulates cell adhesion

作者：Iwasaki Masahiro; Tanaka Ryoichi; Hishiya Akinori; Homma Sachiko; Reed John C; Takayama Shinichi^*

来源：Biochemical and Biophysical Research Communications, 2010, 400(3): 413-418.

DOI：10.1016/j.bbrc.2010.08.092

• Hsp70
• Molecular chaperone
• Rap1
• Guanine nucleotide exchange factor
• WW domain
• Cell adhesion

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 incr

• 出版日期2010-9-24
• 单位河北医科大学