H. M. Bligh Cancer Research Laboratories, Department of Microbiology and Immunology, Chicago Medical School, Rosalind Franklin University of Medicine and Science, North Chicago, Illinois, United States of America.
PLoS Pathog. 2010 Dec 23;6(12):e1001238. doi: 10.1371/journal.ppat.1001238.
KSHV is etiologically associated with Kaposi's sarcoma (KS), an angioproliferative endothelial cell malignancy. Macropinocytosis is the predominant mode of in vitro entry of KSHV into its natural target cells, human dermal microvascular endothelial (HMVEC-d) cells. Although macropinocytosis is known to be a major route of entry for many viruses, the molecule(s) involved in the recruitment and integration of signaling early during macropinosome formation is less well studied. Here we demonstrate that tyrosine phosphorylation of the adaptor protein c-Cbl is required for KSHV induced membrane blebbing and macropinocytosis. KSHV induced the tyrosine phosphorylation of c-Cbl as early as 1 min post-infection and was recruited to the sites of bleb formation. Infection also led to an increase in the interaction of c-Cbl with PI3-K p85 in a time dependent manner. c-Cbl shRNA decreased the formation of KSHV induced membrane blebs and macropinocytosis as well as virus entry. Immunoprecipitation of c-Cbl followed by mass spectrometry identified the interaction of c-Cbl with a novel molecular partner, non-muscle myosin heavy chain IIA (myosin IIA), in bleb associated macropinocytosis. Phosphorylated c-Cbl colocalized with phospho-myosin light chain II in the interior of blebs of infected cells and this interaction was abolished by c-Cbl shRNA. Studies with the myosin II inhibitor blebbistatin demonstrated that myosin IIA is a biologically significant component of the c-Cbl signaling pathway and c-Cbl plays a new role in the recruitment of myosin IIA to the blebs during KSHV infection. Myosin II associates with actin in KSHV induced blebs and the absence of actin and myosin ubiquitination in c-Cbl ShRNA cells suggested that c-Cbl is also responsible for the ubiquitination of these proteins in the infected cells. This is the first study demonstrating the role of c-Cbl in viral entry as well as macropinocytosis, and provides the evidence that a signaling complex containing c-Cbl and myosin IIA plays a crucial role in blebbing and macropinocytosis during viral infection and suggests that targeting c-Cbl could lead to a block in KSHV infection.
卡波氏肉瘤相关疱疹病毒(KSHV)与卡波氏肉瘤(KS)有关,卡波氏肉瘤是一种血管增生性内皮细胞恶性肿瘤。巨胞饮作用是 KSHV 进入其自然靶细胞——人真皮微血管内皮(HMVEC-d)细胞的主要方式。尽管巨胞饮作用是许多病毒进入的主要途径,但在巨胞饮体形成过程中,早期参与招募和整合信号的分子(s)研究得还不够充分。在这里,我们证明衔接蛋白 c-Cbl 的酪氨酸磷酸化是 KSHV 诱导的细胞膜起泡和巨胞饮作用所必需的。KSHV 在感染后 1 分钟内就诱导 c-Cbl 的酪氨酸磷酸化,并被招募到起泡形成的部位。感染还导致 c-Cbl 与 PI3-K p85 的相互作用在时间上呈依赖性增加。c-Cbl shRNA 减少 KSHV 诱导的细胞膜起泡和巨胞饮作用以及病毒进入。c-Cbl 的免疫沉淀后进行质谱分析鉴定出 c-Cbl 与一种新的分子伴侣——非肌肉肌球蛋白重链 IIA(myosin IIA)的相互作用,这种相互作用发生在与巨胞饮作用相关的泡中。磷酸化的 c-Cbl 与感染细胞泡内的磷酸化肌球蛋白轻链 II 共定位,这种相互作用被 c-Cbl shRNA 消除。使用肌球蛋白 II 抑制剂 blebbistatin 的研究表明,肌球蛋白 IIA 是 c-Cbl 信号通路的一个重要组成部分,c-Cbl 在 KSHV 感染期间在泡中招募肌球蛋白 IIA 方面发挥新的作用。肌球蛋白 II 在 KSHV 诱导的泡中与肌动蛋白结合,c-Cbl ShRNA 细胞中肌动蛋白和肌球蛋白的泛素化缺失表明 c-Cbl 也负责感染细胞中这些蛋白的泛素化。这是第一项证明 c-Cbl 在病毒进入以及巨胞饮作用中的作用的研究,为包含 c-Cbl 和肌球蛋白 IIA 的信号复合物在病毒感染期间起泡和巨胞饮作用中发挥关键作用提供了证据,并表明靶向 c-Cbl 可能导致 KSHV 感染受阻。