Grimmer Stine, van Deurs Bo, Sandvig Kirsten
Institute for Cancer Research, The Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway.
J Cell Sci. 2002 Jul 15;115(Pt 14):2953-62. doi: 10.1242/jcs.115.14.2953.
Cholesterol is important for the formation of caveolea and deeply invaginated clathrin-coated pits. We have now investigated whether formation of macropinosomes is dependent on the presence of cholesterol in the plasma membrane. Macropinocytosis in A431 cells was induced by the phorbol ester 12-O-tetradecanoylphorbol 13-acetate, a potent activator of protein kinase C (PKC). When cells were pretreated with methyl-beta-cyclodextrin to extract cholesterol, the phorbol ester was unable to induce the increased endocytosis of ricin otherwise seen, although PKC could still be activated. Electron microscopy revealed that extraction of cholesterol inhibited the formation of membrane ruffles and macropinosomes at the plasma membrane. Furthermore, cholesterol depletion inhibited the phorbol ester-induced reorganization of filamentous actin at the cell periphery, a prerequisite for the formation of membrane ruffles that close into macropinosomes. Under normal conditions the small GTPase Rac1 is activated by the phorbol ester and subsequently localized to the plasma membrane, where it induces the reorganization of actin filaments required for formation of membrane ruffles. Cholesterol depletion did not inhibit the activation of Rac1. However, confocal microscopy showed that extraction of cholesterol prevented the phorbol ester-stimulated localization of Rac1 to the plasma membrane. Thus, our results demonstrate that cholesterol is required for the membrane localization of activated Rac1, actin reorganization, membrane ruffling and macropinocytosis.
胆固醇对于小窝和深陷的网格蛋白包被小窝的形成很重要。我们现在研究了巨胞饮体的形成是否依赖于质膜中胆固醇的存在。用佛波酯12 - O -十四酰佛波醇13 -乙酸酯(一种蛋白激酶C(PKC)的有效激活剂)诱导A431细胞中的巨胞饮作用。当用甲基-β-环糊精预处理细胞以提取胆固醇时,尽管PKC仍可被激活,但佛波酯无法诱导蓖麻毒素内吞作用增加,而在未处理时可以观察到这种增加。电子显微镜显示,胆固醇的提取抑制了质膜处膜皱褶和巨胞饮体的形成。此外,胆固醇耗竭抑制了佛波酯诱导的细胞周边丝状肌动蛋白的重组,而这是膜皱褶闭合形成巨胞饮体的前提条件。在正常条件下,小GTP酶Rac1被佛波酯激活,随后定位于质膜,在那里它诱导形成膜皱褶所需的肌动蛋白丝的重组。胆固醇耗竭并未抑制Rac1的激活。然而,共聚焦显微镜显示,胆固醇的提取阻止了佛波酯刺激的Rac1定位于质膜。因此,我们的结果表明,胆固醇是激活的Rac1的膜定位、肌动蛋白重组、膜皱褶形成和巨胞饮作用所必需的。