Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1

被引:45
|
作者
Xu, XM
Shi, YC
Wu, X
Gambetti, P
Sui, DX
Cui, MZ
机构
[1] Case Western Reserve Univ, Inst Pathol, Cleveland, OH 44106 USA
[2] Michigan State Univ, Dept Biochem, E Lansing, MI 48824 USA
[3] Cleveland Clin Fdn, Dept Cell Biol, Cleveland, OH 44195 USA
关键词
D O I
10.1074/jbc.274.46.32543
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Presenilin-1 (PS-l) is the most causative Alzheimer gene product, and its function is not well understood. In an attempt to elucidate the function of PS-l, we screened a human brain cDNA library for PS-l-interacting proteins using the yeast two-hybrid system and isolated a novel protein containing a PSD-95/Dlg/ZO-1 (PDZ)-like domain. This novel PS l-associated protein (PSAP) shares a significant similarity with a Caenorhabditis elegans protein of unknown function. Northern blot analysis revealed that PSAP is predominantly expressed in the brain. Deletion of the first four C-terminal amino acid residues of PS-l, which contain the PDZ domain-binding motif (Gln-Phe-Tyr-Ile), reduced the binding activity of PS-l toward PSAP 4-fold. These data suggest that PS-l may associate with a PDZ-Iike domain-containing protein in vivo and thus may participate in receptor or channel clustering and intracellular signaling events in the brain.
引用
收藏
页码:32543 / 32546
页数:4
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