Satir B H, Hamasaki T, Reichman M, Murtaugh T J
Department of Anatomy & Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461.
Proc Natl Acad Sci U S A. 1989 Feb;86(3):930-2. doi: 10.1073/pnas.86.3.930.
A cytosolic phosphoprotein that appears to function in membrane fusion during exocytosis of secretory products has previously been isolated from Paramecium tetraurelia. This phosphoprotein, parafusin, with Mr 63,000, is rapidly dephosphorylated via a Ca2+-dependent process when secretagogues induce exocytosis in competent cells. Dephosphorylation does not occur in exocytosis-incompetent cells. Polyclonal antibodies against purified parafusin have now been used to show that this protein is present in unicellular organisms and cells of metazoan groups of wide evolutionary divergence, such as yeast, insects, and mammals, including humans. These results suggest that parafusin was present early in the history of eukaryotes and that it is of functional importance in the general mechanism of exocytosis and membrane fusion.
先前已从四膜虫中分离出一种胞质磷蛋白,该蛋白似乎在分泌产物胞吐过程中的膜融合中发挥作用。这种磷蛋白,即副融合蛋白,分子量为63000,当促分泌素在感受态细胞中诱导胞吐时,它会通过一个Ca2+依赖的过程迅速去磷酸化。在无胞吐能力的细胞中不会发生去磷酸化。现在,针对纯化的副融合蛋白的多克隆抗体已被用于证明该蛋白存在于单细胞生物以及进化差异较大的后生动物类群的细胞中,如酵母、昆虫和包括人类在内的哺乳动物。这些结果表明,副融合蛋白在真核生物历史早期就已存在,并且在胞吐和膜融合的一般机制中具有重要功能。