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Site‐specific phosphorylation of villin remodels the actin cytoskeleton to regulate Sendai viral glycoprotein‐mediated membrane fusion
Author(s) -
Chandra Sunandini,
Kumar Manoj,
Sharma Nishi R.,
Sarkar Debi P.
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13477
Subject(s) - villin , microbiology and biotechnology , cell fusion , phosphorylation , lipid bilayer fusion , actin , sendai virus , actin cytoskeleton , biology , cytoskeleton , dynamin , chemistry , endocytosis , biochemistry , cell , virology , membrane , virus
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 Tyr 499 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 cell‐type dependent phosphorylation in regulating membrane fusion.