@article{awad_fship2_2013,
	title = {{FSHIP2} regulates epithelial cell polarity through its lipid product, which binds to {Dlg1}, a pathway subverted by hepatitis {C} virus core protein},
	volume = {24},
	issn = {1939-4586 (ELECTRONIC); 1059-1524 (LINKING)},
	shorttitle = {{FSHIP2} regulates epithelial cell polarity through its lipid product, which binds to {Dlg1}, a pathway subverted by hepatitis {C} virus core protein},
	abstract = {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.},
	number = {14},
	journal = {Mol Biol Cell},
	author = {Awad, A. and Sar, S. and Barre, R. and Cariven, C. and Marin, M. and Salles, J. P. and Erneux, C. and Samuel, D. and Gassama-Diagne, A.},
	month = jul,
	year = {2013},
	pages = {2171--85},
}

{"_id":"N6anqXyNdTkHxsb3e","bibbaseid":"awad-sar-barre-cariven-marin-salles-erneux-samuel-etal-fship2regulatesepithelialcellpolaritythroughitslipidproductwhichbindstodlg1apathwaysubvertedbyhepatitiscviruscoreprotein-2013","author_short":["Awad, A.","Sar, S.","Barre, R.","Cariven, C.","Marin, M.","Salles, J. P.","Erneux, C.","Samuel, D.","Gassama-Diagne, A."],"bibdata":{"bibtype":"article","type":"article","title":"FSHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein","volume":"24","issn":"1939-4586 (ELECTRONIC); 1059-1524 (LINKING)","shorttitle":"FSHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein","abstract":"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.","number":"14","journal":"Mol Biol Cell","author":[{"propositions":[],"lastnames":["Awad"],"firstnames":["A."],"suffixes":[]},{"propositions":[],"lastnames":["Sar"],"firstnames":["S."],"suffixes":[]},{"propositions":[],"lastnames":["Barre"],"firstnames":["R."],"suffixes":[]},{"propositions":[],"lastnames":["Cariven"],"firstnames":["C."],"suffixes":[]},{"propositions":[],"lastnames":["Marin"],"firstnames":["M."],"suffixes":[]},{"propositions":[],"lastnames":["Salles"],"firstnames":["J.","P."],"suffixes":[]},{"propositions":[],"lastnames":["Erneux"],"firstnames":["C."],"suffixes":[]},{"propositions":[],"lastnames":["Samuel"],"firstnames":["D."],"suffixes":[]},{"propositions":[],"lastnames":["Gassama-Diagne"],"firstnames":["A."],"suffixes":[]}],"month":"July","year":"2013","pages":"2171–85","bibtex":"@article{awad_fship2_2013,\n\ttitle = {{FSHIP2} regulates epithelial cell polarity through its lipid product, which binds to {Dlg1}, a pathway subverted by hepatitis {C} virus core protein},\n\tvolume = {24},\n\tissn = {1939-4586 (ELECTRONIC); 1059-1524 (LINKING)},\n\tshorttitle = {{FSHIP2} regulates epithelial cell polarity through its lipid product, which binds to {Dlg1}, a pathway subverted by hepatitis {C} virus core protein},\n\tabstract = {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.},\n\tnumber = {14},\n\tjournal = {Mol Biol Cell},\n\tauthor = {Awad, A. and Sar, S. and Barre, R. and Cariven, C. and Marin, M. and Salles, J. P. and Erneux, C. and Samuel, D. and Gassama-Diagne, A.},\n\tmonth = jul,\n\tyear = {2013},\n\tpages = {2171--85},\n}\n\n","author_short":["Awad, A.","Sar, S.","Barre, R.","Cariven, C.","Marin, M.","Salles, J. P.","Erneux, C.","Samuel, D.","Gassama-Diagne, A."],"key":"awad_fship2_2013","id":"awad_fship2_2013","bibbaseid":"awad-sar-barre-cariven-marin-salles-erneux-samuel-etal-fship2regulatesepithelialcellpolaritythroughitslipidproductwhichbindstodlg1apathwaysubvertedbyhepatitiscviruscoreprotein-2013","role":"author","urls":{},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"http://bibbase.org/zotero/biblioial","dataSources":["ftoP3zPyb2N3b9Noc"],"keywords":[],"search_terms":["fship2","regulates","epithelial","cell","polarity","through","lipid","product","binds","dlg1","pathway","subverted","hepatitis","virus","core","protein","awad","sar","barre","cariven","marin","salles","erneux","samuel","gassama-diagne"],"title":"FSHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein","year":2013}