Site-specific phosphorylation of villin remodels the actin cytoskeleton to regulate Sendai viral glycoprotein-mediated membrane fusion

FEBS Letters

article

Sunandini Chandra¹  Manoj Kumar¹  Nishi R. Sharma¹  Debi P. Sarkar¹ 

[1] Department of Biochemistry, University of Delhi South Campus

关键词: actin;    host–pathogen interaction;    membrane fusion;    Sendai virosome;    villin;   

DOI  :  10.1002/1873-3468.13477

来源: John Wiley & Sons Ltd.

【 摘 要 】

Connivance of cellular factors during virus-host cell membrane fusion is poorly understood. We have recently shown that cellular villin plays an important role during membrane fusion of reconstituted Sendai virosomes with hepatocytes. Here, we employed villin-null Chinese Hamster Ovary (CHO) cells, where villin expression led to an increased fusion with virosomes, which was further enhanced due to tyrosine phosphorylation in the presence of c-src. However, the villin RRI mutant, lacking actin-severing function, failed to augment membrane fusion. Furthermore, quantitative mass spectrometry and detailed analysis revealed Tyr499 to be the key phosphorylation site of villin responsible for the enhancement of virosome-CHO cell fusion. Overall, our results demonstrate a critical role for villin and its celltype dependent phosphorylation in regulating membrane fusion.

【 授权许可】

Unknown