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Tytuł pozycji:

FSHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein

Tytuł :
FSHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein
Autorzy :
Awad, Aline
Sar, Sokhavuth
Barré, Ronan
Cariven, Clotilde
Marin, Mickael
Salles, Jean Pierre
Erneux, Christophe
Samuel, Didier
Gassama-Diagne, Ama
Pokaż więcej
Temat :
Sciences bio-médicales et agricoles
Sciences exactes et naturelles
Cell Biology of Disease
Sciences de l'ingénieur
Hepacivirus -- physiology
Généralités
Host-Pathogen Interactions
Protein Isoforms -- antagonists & inhibitors -- genetics -- metabolism
Dogs
Phosphatidylinositol Phosphates -- metabolism
Animals
Cell Polarity
Cell Line
Phosphoric Monoester Hydrolases -- antagonists & inhibitors -- genetics -- metabolism
Hepatocytes -- metabolism -- virology
Membrane Proteins -- genetics -- metabolism
Signal Transduction
Epithelial Cells -- metabolism -- virology
Gene Expression Regulation
Phosphatidylinositol 3-Kinases -- genetics -- metabolism
Adaptor Proteins, Signal Transducing -- genetics -- metabolism
RNA, Small Interfering -- genetics -- metabolism
Viral Core Proteins -- genetics -- metabolism
Humans
Phosphatidylinositol 4,5-Diphosphate -- metabolism
Articles
Źródło :
Molecular Biology of the Cell
Molecular biology of the cell, 24 (14
Wydawca :
The American Society for Cell Biology, 2013.
Rok publikacji :
2013
Kolekcja :
DI-fusion_enriched
DI-fusion
Oryginalny identyfikator :
pmc: PMC3708724
pmid: 23699395
Opis pliku :
1 full-text file(s): application/pdf
Język :
English
ISSN :
1939-4586
1059-1524
DOI :
10.1091/mbc.E12-08-0626
The main targets of hepatitis C virus (HCV) are hepatocytes, the highly polarized cells of the liver, and all the steps of its life cycle are tightly dependent on host lipid metabolism. The interplay between polarity and lipid metabolism in HCV infection has been poorly investigated. Signaling lipids, such as phosphoinositides (PIs), play a vital role in polarity, which depends on the distribution and expression of PI kinases and PI phosphatases. In this study, we report that HCV core protein, expressed in Huh7 and Madin-Darby canine kidney (MDCK) cells, disrupts apicobasal polarity. This is associated with decreased expression of the polarity protein Dlg1 and the PI phosphatase SHIP2, which converts phosphatidylinositol 3,4,5-trisphosphate into phosphatidylinositol 4,5-bisphosphate (PtdIns(3,4)P2). SHIP2 is mainly localized at the basolateral membrane of polarized MDCK cells. In addition, PtdIns(3,4)P2 is able to bind to Dlg1. SHIP2 small interfering RNA or its catalytically dead mutant disrupts apicobasal polarity, similar to HCV core. In core-expressing cells, RhoA activity is inhibited, whereas Rac1 is activated. Of interest, SHIP2 expression rescues polarity, RhoA activation, and restricted core level in MDCK cells. We conclude that SHIP2 is an important regulator of polarity, which is subverted by HCV in epithelial cells. It is suggested that SHIP2 could be a promising target for anti-HCV treatment.

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