1. [The interaction of the intracellular domain of beta-amyloid precursor protein with JKTBP2].
- Author
-
Wang WW, Li ZD, Liu RZ, Hong SG, Xu XX, and Chen YG
- Subjects
- Amino Acid Sequence, Amyloid beta-Protein Precursor genetics, Base Sequence, Cell Line, Electrophoresis, Polyacrylamide Gel, Humans, Immunoprecipitation, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Two-Hybrid System Techniques, Amyloid beta-Protein Precursor metabolism, Ribonucleoproteins metabolism
- Abstract
APP (beta-amyloid precursor protein) plays an important role in the formation of Alzheimer's Disease (AD), and its proteolytic product, the intracellular domain AID is believed to be involved in this process by promoting cell apoptosis. To further understand the function of AID in the pathology of AD, we utilized AID as a bait to identify AID interacting proteins in a yeast two-hybrid system. One of the positive clones encodes the fragment corresponding to amino acids 90-204 of heterogeneous nuclear ribonucleoprotein D-like JKTBP2. The interaction between JKTBP2(90)-204 and AID was further confirmed by co-immunoprecipitation in the mammalian 293T cells. These results indicate that JKTBP2 may have an important function in AD formation.
- Published
- 2005