Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance.

Ta-Hsien Lin, Pai-Chi Tsai, Hsin-Tzu Liu, Yi-Chen Chen, Lan-Hsin Wang, Fu-Kai Hsieh, Hsien-Bin Huang

Institute of Biochemistry and Molecular Biology and Structural Biology Program, National Yang-Ming University, Taipei 11221, Taiwan, ROC.

Journal of biochemistry 2005 Dec

filter terms:

KLHY is a short amino-acid sequence of inhibitor-2. This sequence is highly conserved with the protein phosphatase 1 (PP1)-binding consensus motif, RVXF. The role of this segment in binding with PP1 is ambiguous. By using surface plasmon resonance we have characterized its binding ability to PP1. Either site-directed mutagenesis or deletion of KLHY did not significantly affect the dissociation constant between PP1 and inhibitor-2. In comparison with DARPP-32, the deletion of KKIQF, a PP1-binding motif of DARPP-32, resulted in a remarkable reduction in its affinity with PP1. Our results suggested that, compared with the common RVXF motif, the KLHY sequence in intact inhibitor-2 binds weakly to PP1.

Citation

Ta-Hsien Lin, Pai-Chi Tsai, Hsin-Tzu Liu, Yi-Chen Chen, Lan-Hsin Wang, Fu-Kai Hsieh, Hsien-Bin Huang. Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance. Journal of biochemistry. 2005 Dec;138(6):697-700