The chloride intracellular channel protein CLIC4 inhibits filopodium formation induced by constitutively active mutants of formin mDia2
Chloride intracellular channel 4 (CLIC4) functions in diverse actin‐dependent processes. Upon Rho activation, CLIC4 reversibly translocates from the cytosol to the plasma membrane to regulate cell adhesion and migration. At the plasma membrane, CLIC4 counters the formation of filopodia, which requir...
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| Veröffentlicht in: | FEBS letters 2020-06, Vol.594 (11), p.1750-1758 |
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| creator | Argenzio, Elisabetta Innocenti, Metello |
| description | Chloride intracellular channel 4 (CLIC4) functions in diverse actin‐dependent processes. Upon Rho activation, CLIC4 reversibly translocates from the cytosol to the plasma membrane to regulate cell adhesion and migration. At the plasma membrane, CLIC4 counters the formation of filopodia, which requires actin assembly by the formin mammalian Diaphanous (mDia)2. To this end, mDia2 must be activated through conversion from the closed to the open conformation. Thus, CLIC4 could harness the activation or the open conformation of mDia2 to inhibit filopodium formation. Here, we find that CLIC4 silencing enhances the filopodia induced by two constitutively active mDia2 mutants. Furthermore, we report that CLIC4 binds the actin‐regulatory region of mDia2 in vitro. These results suggest that CLIC4 modulates the activity of the open conformation of mDia2, shedding new light into how cells may control filopodia. |
| doi_str_mv | 10.1002/1873-3468.13766 |
| format | Article |
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Upon Rho activation, CLIC4 reversibly translocates from the cytosol to the plasma membrane to regulate cell adhesion and migration. At the plasma membrane, CLIC4 counters the formation of filopodia, which requires actin assembly by the formin mammalian Diaphanous (mDia)2. To this end, mDia2 must be activated through conversion from the closed to the open conformation. Thus, CLIC4 could harness the activation or the open conformation of mDia2 to inhibit filopodium formation. Here, we find that CLIC4 silencing enhances the filopodia induced by two constitutively active mDia2 mutants. Furthermore, we report that CLIC4 binds the actin‐regulatory region of mDia2 in vitro. These results suggest that CLIC4 modulates the activity of the open conformation of mDia2, shedding new light into how cells may control filopodia.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.13766</identifier><identifier>PMID: 32145706</identifier><language>eng</language><publisher>England</publisher><subject>actin ; Actins - metabolism ; Chloride Channels - deficiency ; Chloride Channels - genetics ; Chloride Channels - metabolism ; CLIC4 ; cytoskeleton ; filopodia ; formins ; Formins - chemistry ; Formins - genetics ; Formins - metabolism ; HeLa Cells ; Humans ; mDia2 ; Mutation ; Pseudopodia - metabolism</subject><ispartof>FEBS letters, 2020-06, Vol.594 (11), p.1750-1758</ispartof><rights>2020 The Authors. published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies</rights><rights>2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3856-38c8c5017d0cae205959f7a0270435d52dc2d3c66bf9be9fe8f597fddd2dead03</citedby><cites>FETCH-LOGICAL-c3856-38c8c5017d0cae205959f7a0270435d52dc2d3c66bf9be9fe8f597fddd2dead03</cites><orcidid>0000-0002-7455-2559</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F1873-3468.13766$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F1873-3468.13766$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32145706$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Argenzio, Elisabetta</creatorcontrib><creatorcontrib>Innocenti, Metello</creatorcontrib><title>The chloride intracellular channel protein CLIC4 inhibits filopodium formation induced by constitutively active mutants of formin mDia2</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Chloride intracellular channel 4 (CLIC4) functions in diverse actin‐dependent processes. Upon Rho activation, CLIC4 reversibly translocates from the cytosol to the plasma membrane to regulate cell adhesion and migration. At the plasma membrane, CLIC4 counters the formation of filopodia, which requires actin assembly by the formin mammalian Diaphanous (mDia)2. To this end, mDia2 must be activated through conversion from the closed to the open conformation. Thus, CLIC4 could harness the activation or the open conformation of mDia2 to inhibit filopodium formation. Here, we find that CLIC4 silencing enhances the filopodia induced by two constitutively active mDia2 mutants. Furthermore, we report that CLIC4 binds the actin‐regulatory region of mDia2 in vitro. These results suggest that CLIC4 modulates the activity of the open conformation of mDia2, shedding new light into how cells may control filopodia.</description><subject>actin</subject><subject>Actins - metabolism</subject><subject>Chloride Channels - deficiency</subject><subject>Chloride Channels - genetics</subject><subject>Chloride Channels - metabolism</subject><subject>CLIC4</subject><subject>cytoskeleton</subject><subject>filopodia</subject><subject>formins</subject><subject>Formins - chemistry</subject><subject>Formins - genetics</subject><subject>Formins - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>mDia2</subject><subject>Mutation</subject><subject>Pseudopodia - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>EIF</sourceid><recordid>eNqFkM1u3CAUhVHUqpmmXXdXsezGCT_G2Mt28tNII3WTrhGGi4YImyngVvMEfe3gTJptV8DlO0e6H0KfKLmkhLAr2kve8LbrLymXXXeGNq-TN2hDCG0bIQd-jt7n_Ejqu6fDO3TOGW2FJN0G_X3YAzb7EJO3gP1ckjYQwhJ0qmM9zxDwIcUCfsbb3f22rczej75k7HyIh2j9MmEX06SLj3P9tYsBi8cjNnHOxZel-N8Qjlib9YKnpei5pqN7TtXa6dpr9gG9dTpk-PhyXqCftzcP2-_N7sfd_fbrrjG8F13De9MbQai0xGhgRAxicFITJknLhRXMGma56brRDSMMDnonBumstcyCtoRfoC-n3rrUrwVyUZPP68Z6hrhkxbhsed-2TFT06oSaFHNO4NQh-Umno6JErfbV6lqtrtWz_Zr4_FK-jBPYV_6f7gp0J-CPD3D8X5-6vfnGTs1PJc2SFA</recordid><startdate>202006</startdate><enddate>202006</enddate><creator>Argenzio, Elisabetta</creator><creator>Innocenti, Metello</creator><scope>24P</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-7455-2559</orcidid></search><sort><creationdate>202006</creationdate><title>The chloride intracellular channel protein CLIC4 inhibits filopodium formation induced by constitutively active mutants of formin mDia2</title><author>Argenzio, Elisabetta ; Innocenti, Metello</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3856-38c8c5017d0cae205959f7a0270435d52dc2d3c66bf9be9fe8f597fddd2dead03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>actin</topic><topic>Actins - metabolism</topic><topic>Chloride Channels - deficiency</topic><topic>Chloride Channels - genetics</topic><topic>Chloride Channels - metabolism</topic><topic>CLIC4</topic><topic>cytoskeleton</topic><topic>filopodia</topic><topic>formins</topic><topic>Formins - chemistry</topic><topic>Formins - genetics</topic><topic>Formins - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>mDia2</topic><topic>Mutation</topic><topic>Pseudopodia - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Argenzio, Elisabetta</creatorcontrib><creatorcontrib>Innocenti, Metello</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Argenzio, Elisabetta</au><au>Innocenti, Metello</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The chloride intracellular channel protein CLIC4 inhibits filopodium formation induced by constitutively active mutants of formin mDia2</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2020-06</date><risdate>2020</risdate><volume>594</volume><issue>11</issue><spage>1750</spage><epage>1758</epage><pages>1750-1758</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Chloride intracellular channel 4 (CLIC4) functions in diverse actin‐dependent processes. Upon Rho activation, CLIC4 reversibly translocates from the cytosol to the plasma membrane to regulate cell adhesion and migration. At the plasma membrane, CLIC4 counters the formation of filopodia, which requires actin assembly by the formin mammalian Diaphanous (mDia)2. To this end, mDia2 must be activated through conversion from the closed to the open conformation. Thus, CLIC4 could harness the activation or the open conformation of mDia2 to inhibit filopodium formation. Here, we find that CLIC4 silencing enhances the filopodia induced by two constitutively active mDia2 mutants. Furthermore, we report that CLIC4 binds the actin‐regulatory region of mDia2 in vitro. 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| source | Wiley Free Content; Wiley Online Library - AutoHoldings Journals; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | actin Actins - metabolism Chloride Channels - deficiency Chloride Channels - genetics Chloride Channels - metabolism CLIC4 cytoskeleton filopodia formins Formins - chemistry Formins - genetics Formins - metabolism HeLa Cells Humans mDia2 Mutation Pseudopodia - metabolism |
| title | The chloride intracellular channel protein CLIC4 inhibits filopodium formation induced by constitutively active mutants of formin mDia2 |
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