Nakayama T, Yaoi T, Kuwajima G, Yoshie O, Sakata T
Department of Bacteriology, Kinki University School of Medicine, Osaka-Sayama, Osaka, Japan.
FEBS Lett. 1999 Jun 18;453(1-2):77-80. doi: 10.1016/s0014-5793(99)00700-0.
N-copine is a novel two C2 domain protein that shows Ca2(+)-dependent phospholipid binding and membrane association. By using yeast two-hybrid assays, we identified OS-9 as a protein capable of interacting with N-copine. We further revealed that the second C2 domain of N-copine bound with the carboxy-terminal region of OS-9. Their interaction in vivo was also confirmed by co-immunoprecipitation from 293E cells co-expressing transfected N-copine and OS-9. In vitro binding assays showed that this interaction was Ca2(+)-dependent. By Northern blot analysis, N-copine and OS-9 were co-expressed in the same regions of human brain. These results reveal that OS-9 is a potential target of N-copine.
N-柯平蛋白是一种新型的含有两个C2结构域的蛋白质,具有Ca2+依赖性磷脂结合和膜结合特性。通过酵母双杂交实验,我们鉴定出OS-9是一种能够与N-柯平蛋白相互作用的蛋白质。我们进一步发现,N-柯平蛋白的第二个C2结构域与OS-9的羧基末端区域结合。在共表达转染的N-柯平蛋白和OS-9的293E细胞中进行的免疫共沉淀实验也证实了它们在体内的相互作用。体外结合实验表明,这种相互作用是Ca2+依赖性的。通过Northern印迹分析,N-柯平蛋白和OS-9在人类大脑的相同区域共表达。这些结果表明,OS-9是N-柯平蛋白的潜在靶点。