异戊二烯化的Rab3A与两个Rabphilin-3A分子形成异源四聚体。

Heterotetramer formation of prenylated Rab3A with two Rabphilin-3A molecules.

作者信息

Takahashi K, Sasaki T, Takai Y

机构信息

Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita, Japan.

出版信息

Biochem Biophys Res Commun. 1995 Dec 26;217(3):979-86. doi: 10.1006/bbrc.1995.2866.

DOI:10.1006/bbrc.1995.2866

PMID:8554624

Abstract

Rab3A small GTP-binding protein and its putative target protein, named Rabphilin-3A, are implicated in neurotransmitter release. We have investigated here the function of the lipid modifications of Rab3A (Mr approximately 25,000) in its interaction with Rabphilin-3A (Mr approximately 80,000). Lipid-modified GTP-Rab3A dimerized and lipid-unmodified one monomerized. Lipid-modified GTP-Rab3A (Mr approximately 50,000) formed a heterotetramer (Mr approximately 210,000) with two Rabphilin-3A molecules, whereas lipid-unmodified GTP-Rab3A formed a heterodimer (Mr approximately 105,000) with one Rabphilin-3A molecule. These results indicate that two lipid-modified GTP-Rab3A molecules form a heterotetramer with two Rabphilin-3A molecules.

摘要

Rab3A小GTP结合蛋白及其推定的靶蛋白Rabphilin-3A与神经递质释放有关。我们在此研究了Rab3A（分子量约25,000）的脂质修饰在其与Rabphilin-3A（分子量约80,000）相互作用中的功能。脂质修饰的GTP-Rab3A形成二聚体，未进行脂质修饰的则形成单体。脂质修饰的GTP-Rab3A（分子量约50,000）与两个Rabphilin-3A分子形成异源四聚体（分子量约210,000），而未进行脂质修饰的GTP-Rab3A与一个Rabphilin-3A分子形成异源二聚体（分子量约105,000）。这些结果表明，两个脂质修饰的GTP-Rab3A分子与两个Rabphilin-3A分子形成异源四聚体。