Sasaki T, Kaibuchi K, Kabcenell A K, Novick P J, Takai Y
Department of Biochemistry, Kobe University School of Medicine, Japan.
Mol Cell Biol. 1991 May;11(5):2909-12. doi: 10.1128/mcb.11.5.2909-2912.1991.
Evidence is accumulating that smg p25A, a small GTP-binding protein, may be involved in the regulated secretory processes of mammalian cells. The SEC4 protein is known to be required for constitutive secretion in yeast cells. We show here that the mammalian GDP dissociation inhibitor (GDI), which was identified by its action on smg p25A, is active on the yeast SEC4 protein in inhibiting the GDP/GTP exchange reaction and is capable of forming a complex with the GDP-bound form of the SEC4 protein but not with the GTP-bound form. These results together with our previous findings that smg p25A GDI is found in mammalian cells with both regulated and constitutive secretion types suggest that smg p25A GDI plays a role in both regulated and constitutive secretory processes, although smg p25A itself may be involved only in regulated secretory processes. These results also suggest that a GDI for the SEC4 protein is present in yeast cells.
越来越多的证据表明,小GTP结合蛋白smg p25A可能参与哺乳动物细胞的调节性分泌过程。已知SEC4蛋白是酵母细胞组成型分泌所必需的。我们在此表明,通过其对smg p25A的作用鉴定出的哺乳动物GDP解离抑制剂(GDI),对酵母SEC4蛋白具有抑制GDP/GTP交换反应的活性,并且能够与SEC4蛋白的GDP结合形式形成复合物,但不能与GTP结合形式形成复合物。这些结果与我们之前的发现一起,即smg p25A GDI存在于具有调节性和组成型分泌类型的哺乳动物细胞中,表明smg p25A GDI在调节性和组成型分泌过程中均起作用,尽管smg p25A本身可能仅参与调节性分泌过程。这些结果还表明酵母细胞中存在SEC4蛋白的GDI。