TY - JOUR
T1 - The interaction between ADAM 22 and 14-3-3ζ
T2 - Regulation of cell adhesion and spreading
AU - Zhu, Peng Cheng
AU - Sun, Yubo
AU - Xu, Rener
AU - Sang, Yingying
AU - Zhao, Jing
AU - Liu, Gang
AU - Cai, Liang
AU - Li, Changben
AU - Zhao, Shouyuan
N1 - Funding Information:
This work was supported by a National Natural Sciences Foundation of China Grant 30170866 to Y.Z., and in part by a National Institutes of Health Grant AR 26599 to Y.S.
PY - 2003/2/21
Y1 - 2003/2/21
N2 - The ADAM family consists of a number of transmembrane proteins that contain disintegrin-like and metalloproteinase-like domains. Therefore, ADAMs potentially have cell adhesion and protease activities. 14-3-3 proteins are a highly conserved family of cytoplasmic proteins that associate with several intracellular signaling molecules in the regulation of various cellular functions. Here we report the identification of a novel interaction between the ADAM 22 cytoplasmic tail and the 14-3-3ζ isoform by a yeast two-hybrid screen. The interaction between the ADAM 22 cytoplasmic tail and 14-3-3ζ was confirmed by an in vitro protein pull-down assay as well as by co-immunoprecipitation, and the binding sites were mapped to the 28 amino acid residues of the C-terminus of the ADAM 22 cytoplasmic tail. Furthermore, we found that overexpression of the ADAM 22 cytoplasmic tail in human SGH44 cells inhibited cell adhesion and spreading and that deletion or mutation of the binding site for 14-3-3ζ within the ADAM 22 cytoplasmic tail abolished the ability of the overexpressed cytoplasmic tail to alter cell adhesion and spreading. Taken together, these results for the first time demonstrate an association between ADAM 22 and a 14-3-3 protein and suggest a potential role for the 14-3-3ζ/ADAM 22 association in the regulation of cell adhesion and related signaling events.
AB - The ADAM family consists of a number of transmembrane proteins that contain disintegrin-like and metalloproteinase-like domains. Therefore, ADAMs potentially have cell adhesion and protease activities. 14-3-3 proteins are a highly conserved family of cytoplasmic proteins that associate with several intracellular signaling molecules in the regulation of various cellular functions. Here we report the identification of a novel interaction between the ADAM 22 cytoplasmic tail and the 14-3-3ζ isoform by a yeast two-hybrid screen. The interaction between the ADAM 22 cytoplasmic tail and 14-3-3ζ was confirmed by an in vitro protein pull-down assay as well as by co-immunoprecipitation, and the binding sites were mapped to the 28 amino acid residues of the C-terminus of the ADAM 22 cytoplasmic tail. Furthermore, we found that overexpression of the ADAM 22 cytoplasmic tail in human SGH44 cells inhibited cell adhesion and spreading and that deletion or mutation of the binding site for 14-3-3ζ within the ADAM 22 cytoplasmic tail abolished the ability of the overexpressed cytoplasmic tail to alter cell adhesion and spreading. Taken together, these results for the first time demonstrate an association between ADAM 22 and a 14-3-3 protein and suggest a potential role for the 14-3-3ζ/ADAM 22 association in the regulation of cell adhesion and related signaling events.
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U2 - 10.1016/S0006-291X(03)00056-1
DO - 10.1016/S0006-291X(03)00056-1
M3 - Article
C2 - 12589811
AN - SCOPUS:0037459098
SN - 0006-291X
VL - 301
SP - 991
EP - 999
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -