Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration
While there is circumstantial evidence to suggest a requirement for phospholipase C-gamma(1) (PLC-gamma(1)) in actin reorganization and cell migration, few studies have examined the direct mechanisms that link regulators of the actin cytoskeleton with this crucial signaling molecule. This study was...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 2007-05, Vol.292 (5), p.C1775-C1786 |
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| container_title | American Journal of Physiology: Cell Physiology |
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| creator | Wang, Yaohong Tomar, Alok George, Sudeep P Khurana, Seema |
| description | While there is circumstantial evidence to suggest a requirement for phospholipase C-gamma(1) (PLC-gamma(1)) in actin reorganization and cell migration, few studies have examined the direct mechanisms that link regulators of the actin cytoskeleton with this crucial signaling molecule. This study was aimed to examine the role that villin, an epithelial cell-specific actin-binding protein, and its ligand PLC-gamma(1) play in migration in intestinal and renal epithelial cell lines that endogenously or ectopically express human villin. Basal as well as epidermal growth factor (EGF)-stimulated cell migration was accompanied by tyrosine phosphorylation of villin and its association with PLC-gamma(1). Inhibition of villin phosphorylation prevented villin-PLC-gamma(1) complex formation as well as villin-induced cell migration. The absolute requirement for PLC-gamma(1) in villin-induced cell migration was demonstrated by measuring cell motility in PLC-gamma(1)(-/-) cells and by downregulation of endogenous PLC-gamma(1). EGF-stimulated direct interaction of villin with the Src homology domain 2 domain of PLC-gamma(1) at the plasma membrane was demonstrated in living cells by using fluorescence resonance energy transfer. These results demonstrate that villin provides an important link between the activation of phosphoinositide signal transduction pathway and epithelial cell migration. |
| doi_str_mv | 10.1152/ajpcell.00420.2006 |
| format | Article |
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This study was aimed to examine the role that villin, an epithelial cell-specific actin-binding protein, and its ligand PLC-gamma(1) play in migration in intestinal and renal epithelial cell lines that endogenously or ectopically express human villin. Basal as well as epidermal growth factor (EGF)-stimulated cell migration was accompanied by tyrosine phosphorylation of villin and its association with PLC-gamma(1). Inhibition of villin phosphorylation prevented villin-PLC-gamma(1) complex formation as well as villin-induced cell migration. The absolute requirement for PLC-gamma(1) in villin-induced cell migration was demonstrated by measuring cell motility in PLC-gamma(1)(-/-) cells and by downregulation of endogenous PLC-gamma(1). EGF-stimulated direct interaction of villin with the Src homology domain 2 domain of PLC-gamma(1) at the plasma membrane was demonstrated in living cells by using fluorescence resonance energy transfer. These results demonstrate that villin provides an important link between the activation of phosphoinositide signal transduction pathway and epithelial cell migration.</description><identifier>ISSN: 0363-6143</identifier><identifier>DOI: 10.1152/ajpcell.00420.2006</identifier><identifier>PMID: 17229814</identifier><language>eng</language><publisher>United States</publisher><subject>Actins - metabolism ; Animals ; Caco-2 Cells ; Cell Membrane - metabolism ; Cell Movement - drug effects ; Dogs ; Epidermal Growth Factor - metabolism ; Epithelial Cells - drug effects ; Epithelial Cells - enzymology ; Epithelial Cells - metabolism ; Estrenes - pharmacology ; Fluorescence Resonance Energy Transfer ; Hepatocyte Growth Factor - metabolism ; Humans ; Intestinal Mucosa - metabolism ; Intestinal Mucosa - pathology ; Kidney - cytology ; Kidney - metabolism ; Mice ; Microfilament Proteins - genetics ; Microfilament Proteins - metabolism ; Mutation ; Phospholipase C gamma - antagonists & inhibitors ; Phospholipase C gamma - genetics ; Phospholipase C gamma - metabolism ; Phosphorylation ; Protein Kinase Inhibitors - pharmacology ; Pyrimidines - pharmacology ; Pyrrolidinones - pharmacology ; RNA, Small Interfering - genetics ; RNA, Small Interfering - metabolism ; Signal Transduction - drug effects ; src Homology Domains ; src-Family Kinases - antagonists & inhibitors ; src-Family Kinases - metabolism ; Transfection ; Tyrosine - metabolism ; Wound Healing - drug effects</subject><ispartof>American Journal of Physiology: Cell Physiology, 2007-05, Vol.292 (5), p.C1775-C1786</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27931,27932</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17229814$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Yaohong</creatorcontrib><creatorcontrib>Tomar, Alok</creatorcontrib><creatorcontrib>George, Sudeep P</creatorcontrib><creatorcontrib>Khurana, Seema</creatorcontrib><title>Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration</title><title>American Journal of Physiology: Cell Physiology</title><addtitle>Am J Physiol Cell Physiol</addtitle><description>While there is circumstantial evidence to suggest a requirement for phospholipase C-gamma(1) (PLC-gamma(1)) in actin reorganization and cell migration, few studies have examined the direct mechanisms that link regulators of the actin cytoskeleton with this crucial signaling molecule. This study was aimed to examine the role that villin, an epithelial cell-specific actin-binding protein, and its ligand PLC-gamma(1) play in migration in intestinal and renal epithelial cell lines that endogenously or ectopically express human villin. Basal as well as epidermal growth factor (EGF)-stimulated cell migration was accompanied by tyrosine phosphorylation of villin and its association with PLC-gamma(1). Inhibition of villin phosphorylation prevented villin-PLC-gamma(1) complex formation as well as villin-induced cell migration. The absolute requirement for PLC-gamma(1) in villin-induced cell migration was demonstrated by measuring cell motility in PLC-gamma(1)(-/-) cells and by downregulation of endogenous PLC-gamma(1). EGF-stimulated direct interaction of villin with the Src homology domain 2 domain of PLC-gamma(1) at the plasma membrane was demonstrated in living cells by using fluorescence resonance energy transfer. These results demonstrate that villin provides an important link between the activation of phosphoinositide signal transduction pathway and epithelial cell migration.</description><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Caco-2 Cells</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Movement - drug effects</subject><subject>Dogs</subject><subject>Epidermal Growth Factor - metabolism</subject><subject>Epithelial Cells - drug effects</subject><subject>Epithelial Cells - enzymology</subject><subject>Epithelial Cells - metabolism</subject><subject>Estrenes - pharmacology</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>Hepatocyte Growth Factor - metabolism</subject><subject>Humans</subject><subject>Intestinal Mucosa - metabolism</subject><subject>Intestinal Mucosa - pathology</subject><subject>Kidney - cytology</subject><subject>Kidney - metabolism</subject><subject>Mice</subject><subject>Microfilament Proteins - genetics</subject><subject>Microfilament Proteins - metabolism</subject><subject>Mutation</subject><subject>Phospholipase C gamma - antagonists & inhibitors</subject><subject>Phospholipase C gamma - genetics</subject><subject>Phospholipase C gamma - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinase Inhibitors - pharmacology</subject><subject>Pyrimidines - pharmacology</subject><subject>Pyrrolidinones - pharmacology</subject><subject>RNA, Small Interfering - genetics</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Signal Transduction - drug effects</subject><subject>src Homology Domains</subject><subject>src-Family Kinases - antagonists & inhibitors</subject><subject>src-Family Kinases - metabolism</subject><subject>Transfection</subject><subject>Tyrosine - metabolism</subject><subject>Wound Healing - drug effects</subject><issn>0363-6143</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1ULtOwzAA9ACipfADDMgTgiHBr9jJiCpeUqUuILFFtmO3rpzY2AlS_55WlOF0w53uTgfADUYlxhV5lLuojfclQoygkiDEz8AcUU4Ljhmdgcucd-go8uYCzLAgpKkxm4OvtfJuI8eQ9jAFb6ANCcZtyAd4F2U2cFlsZN_Le_wA3QB_nPduKNzQTdp00EQ3bo130sNjP-zdJsnRheEKnFvps7k-8QJ8vjx_LN-K1fr1ffm0KiKmzVgwRRjVoia8QppJYYXEtiE1row2mJvOWKutpQJVkihVC9pRgiuhlBJai4YuwN1fbkzhezJ5bHuXj1PkYMKUW4FYgwlnB-PtyTip3nRtTK6Xad_-f0F_AUKfYV0</recordid><startdate>200705</startdate><enddate>200705</enddate><creator>Wang, Yaohong</creator><creator>Tomar, Alok</creator><creator>George, Sudeep P</creator><creator>Khurana, Seema</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200705</creationdate><title>Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration</title><author>Wang, Yaohong ; Tomar, Alok ; George, Sudeep P ; Khurana, Seema</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p139t-4b243c782650c4a7f7a1f92815ece16edeffcff3705a2bb873d32157bbb7cc793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Caco-2 Cells</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Movement - drug effects</topic><topic>Dogs</topic><topic>Epidermal Growth Factor - metabolism</topic><topic>Epithelial Cells - drug effects</topic><topic>Epithelial Cells - enzymology</topic><topic>Epithelial Cells - metabolism</topic><topic>Estrenes - pharmacology</topic><topic>Fluorescence Resonance Energy Transfer</topic><topic>Hepatocyte Growth Factor - metabolism</topic><topic>Humans</topic><topic>Intestinal Mucosa - metabolism</topic><topic>Intestinal Mucosa - pathology</topic><topic>Kidney - cytology</topic><topic>Kidney - metabolism</topic><topic>Mice</topic><topic>Microfilament Proteins - genetics</topic><topic>Microfilament Proteins - metabolism</topic><topic>Mutation</topic><topic>Phospholipase C gamma - antagonists & inhibitors</topic><topic>Phospholipase C gamma - genetics</topic><topic>Phospholipase C gamma - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinase Inhibitors - pharmacology</topic><topic>Pyrimidines - pharmacology</topic><topic>Pyrrolidinones - pharmacology</topic><topic>RNA, Small Interfering - genetics</topic><topic>RNA, Small Interfering - metabolism</topic><topic>Signal Transduction - drug effects</topic><topic>src Homology Domains</topic><topic>src-Family Kinases - antagonists & inhibitors</topic><topic>src-Family Kinases - metabolism</topic><topic>Transfection</topic><topic>Tyrosine - metabolism</topic><topic>Wound Healing - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Yaohong</creatorcontrib><creatorcontrib>Tomar, Alok</creatorcontrib><creatorcontrib>George, Sudeep P</creatorcontrib><creatorcontrib>Khurana, Seema</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>American Journal of Physiology: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Yaohong</au><au>Tomar, Alok</au><au>George, Sudeep P</au><au>Khurana, Seema</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><addtitle>Am J Physiol Cell Physiol</addtitle><date>2007-05</date><risdate>2007</risdate><volume>292</volume><issue>5</issue><spage>C1775</spage><epage>C1786</epage><pages>C1775-C1786</pages><issn>0363-6143</issn><abstract>While there is circumstantial evidence to suggest a requirement for phospholipase C-gamma(1) (PLC-gamma(1)) in actin reorganization and cell migration, few studies have examined the direct mechanisms that link regulators of the actin cytoskeleton with this crucial signaling molecule. This study was aimed to examine the role that villin, an epithelial cell-specific actin-binding protein, and its ligand PLC-gamma(1) play in migration in intestinal and renal epithelial cell lines that endogenously or ectopically express human villin. Basal as well as epidermal growth factor (EGF)-stimulated cell migration was accompanied by tyrosine phosphorylation of villin and its association with PLC-gamma(1). Inhibition of villin phosphorylation prevented villin-PLC-gamma(1) complex formation as well as villin-induced cell migration. The absolute requirement for PLC-gamma(1) in villin-induced cell migration was demonstrated by measuring cell motility in PLC-gamma(1)(-/-) cells and by downregulation of endogenous PLC-gamma(1). EGF-stimulated direct interaction of villin with the Src homology domain 2 domain of PLC-gamma(1) at the plasma membrane was demonstrated in living cells by using fluorescence resonance energy transfer. These results demonstrate that villin provides an important link between the activation of phosphoinositide signal transduction pathway and epithelial cell migration.</abstract><cop>United States</cop><pmid>17229814</pmid><doi>10.1152/ajpcell.00420.2006</doi></addata></record> |
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| subjects | Actins - metabolism Animals Caco-2 Cells Cell Membrane - metabolism Cell Movement - drug effects Dogs Epidermal Growth Factor - metabolism Epithelial Cells - drug effects Epithelial Cells - enzymology Epithelial Cells - metabolism Estrenes - pharmacology Fluorescence Resonance Energy Transfer Hepatocyte Growth Factor - metabolism Humans Intestinal Mucosa - metabolism Intestinal Mucosa - pathology Kidney - cytology Kidney - metabolism Mice Microfilament Proteins - genetics Microfilament Proteins - metabolism Mutation Phospholipase C gamma - antagonists & inhibitors Phospholipase C gamma - genetics Phospholipase C gamma - metabolism Phosphorylation Protein Kinase Inhibitors - pharmacology Pyrimidines - pharmacology Pyrrolidinones - pharmacology RNA, Small Interfering - genetics RNA, Small Interfering - metabolism Signal Transduction - drug effects src Homology Domains src-Family Kinases - antagonists & inhibitors src-Family Kinases - metabolism Transfection Tyrosine - metabolism Wound Healing - drug effects |
| title | Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration |
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