The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?
Chloride intracellular channel proteins (CLICs) are distinct from most ion channels in that they have both soluble and integral membrane forms. CLICs are highly conserved in chordates, with six vertebrate paralogues. CLIC-like proteins are found in other metazoans. CLICs form channels in artificial...
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| Veröffentlicht in: | FEBS letters 2010-05, Vol.584 (10), p.2093-2101 |
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| creator | Littler, Dene R. Harrop, Stephen J. Goodchild, Sophia C. Phang, Juanita M. Mynott, Andrew V. Jiang, Lele Valenzuela, Stella M. Mazzanti, Michele Brown, Louise J. Breit, Samuel N. Curmi, Paul M.G. |
| description | Chloride intracellular channel proteins (CLICs) are distinct from most ion channels in that they have both soluble and integral membrane forms. CLICs are highly conserved in chordates, with six vertebrate paralogues. CLIC-like proteins are found in other metazoans. CLICs form channels in artificial bilayers in a process favoured by oxidising conditions and low pH. They are structurally plastic, with CLIC1 adopting two distinct soluble conformations. Phylogenetic and structural data indicate that CLICs are likely to have enzymatic function. The physiological role of CLICs appears to be maintenance of intracellular membranes, which is associated with tubulogenesis but may involve other substructures. |
| doi_str_mv | 10.1016/j.febslet.2010.01.027 |
| format | Article |
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CLICs are highly conserved in chordates, with six vertebrate paralogues. CLIC-like proteins are found in other metazoans. CLICs form channels in artificial bilayers in a process favoured by oxidising conditions and low pH. They are structurally plastic, with CLIC1 adopting two distinct soluble conformations. Phylogenetic and structural data indicate that CLICs are likely to have enzymatic function. The physiological role of CLICs appears to be maintenance of intracellular membranes, which is associated with tubulogenesis but may involve other substructures.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2010.01.027</identifier><identifier>PMID: 20085760</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Cell Membrane - metabolism ; Chloride Channels - chemistry ; Chloride Channels - classification ; Chloride Channels - genetics ; Chloride Channels - metabolism ; chloride intracellular channel ; Chloride intracellular channel protein ; Chordata ; CLIC ; CLIC1 ; Cytoskeleton - metabolism ; dehydroascorbate reductase ; DHAR ; endoplasmic reticulum ; Enzymes - chemistry ; Enzymes - classification ; Enzymes - genetics ; Enzymes - metabolism ; ERM ; ezrin–moesin–radixin ; glutaredoxin ; glutathione ; glutathione S-transferase ; Grx ; GSH ; GST ; GST omega ; GSTO ; Humans ; Hydrogen-Ion Concentration ; Membrane insertion ; Metazoa ; Oxidation-Reduction ; Redox ; transmembrane ; Tubulogenesis</subject><ispartof>FEBS letters, 2010-05, Vol.584 (10), p.2093-2101</ispartof><rights>2010 Federation of European Biochemical Societies</rights><rights>FEBS Letters 584 (2010) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5275-4a66e8f6cd37d29a83280720c3e9c594acabf8576fd8594eea2305f4a9907ef53</citedby><cites>FETCH-LOGICAL-c5275-4a66e8f6cd37d29a83280720c3e9c594acabf8576fd8594eea2305f4a9907ef53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2010.01.027$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579310000505$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20085760$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Littler, Dene R.</creatorcontrib><creatorcontrib>Harrop, Stephen J.</creatorcontrib><creatorcontrib>Goodchild, Sophia C.</creatorcontrib><creatorcontrib>Phang, Juanita M.</creatorcontrib><creatorcontrib>Mynott, Andrew V.</creatorcontrib><creatorcontrib>Jiang, Lele</creatorcontrib><creatorcontrib>Valenzuela, Stella M.</creatorcontrib><creatorcontrib>Mazzanti, Michele</creatorcontrib><creatorcontrib>Brown, Louise J.</creatorcontrib><creatorcontrib>Breit, Samuel N.</creatorcontrib><creatorcontrib>Curmi, Paul M.G.</creatorcontrib><title>The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Chloride intracellular channel proteins (CLICs) are distinct from most ion channels in that they have both soluble and integral membrane forms. CLICs are highly conserved in chordates, with six vertebrate paralogues. CLIC-like proteins are found in other metazoans. CLICs form channels in artificial bilayers in a process favoured by oxidising conditions and low pH. They are structurally plastic, with CLIC1 adopting two distinct soluble conformations. Phylogenetic and structural data indicate that CLICs are likely to have enzymatic function. The physiological role of CLICs appears to be maintenance of intracellular membranes, which is associated with tubulogenesis but may involve other substructures.</description><subject>Animals</subject><subject>Cell Membrane - metabolism</subject><subject>Chloride Channels - chemistry</subject><subject>Chloride Channels - classification</subject><subject>Chloride Channels - genetics</subject><subject>Chloride Channels - metabolism</subject><subject>chloride intracellular channel</subject><subject>Chloride intracellular channel protein</subject><subject>Chordata</subject><subject>CLIC</subject><subject>CLIC1</subject><subject>Cytoskeleton - metabolism</subject><subject>dehydroascorbate reductase</subject><subject>DHAR</subject><subject>endoplasmic reticulum</subject><subject>Enzymes - chemistry</subject><subject>Enzymes - classification</subject><subject>Enzymes - genetics</subject><subject>Enzymes - metabolism</subject><subject>ERM</subject><subject>ezrin–moesin–radixin</subject><subject>glutaredoxin</subject><subject>glutathione</subject><subject>glutathione S-transferase</subject><subject>Grx</subject><subject>GSH</subject><subject>GST</subject><subject>GST omega</subject><subject>GSTO</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Membrane insertion</subject><subject>Metazoa</subject><subject>Oxidation-Reduction</subject><subject>Redox</subject><subject>transmembrane</subject><subject>Tubulogenesis</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1PGzEQhq0KVALtT2i1Ny7ZMLbXa7sXRCMokSJxgB4ry_GOwdF-0PWmbfj19SohVzjZM_POO2M_hHyhMKNAy4v1zOMq1jjMGKQc0Bkw-YFMqJI850WpjsgEgBa5kJqfkNMY15BiRfVHcsIAlJAlTMivhyfMsA2Pjc06nw0pmi8X8-y57wYMbfyWLbo2c0-2bbGO06zHqvt3qE5T68u2wXSJznrf1VVoHw_ly0_k2Ns64uf9eUZ-3lw_zG_z5d2PxfxqmTvBpMgLW5aofOkqLiumreJMgWTgOGondGGdXflxYV-pFCJaxkH4wmoNEr3gZ-R855sm_95gHEwTosO6ti12m2g0VVBQUOxNpeQclAItk1LslK7vYuzRm-c-NLbfGgpmRGDWZo_AjAgMUJMQpL6v-wmbVYPVoev1z5Pgdif4G2rcvs_V3Fx_Z_cjzxEnTSRBwPjuy51VYoN_AvYmuoCtwyr06AZTdeGNbf8DvTeupQ</recordid><startdate>20100517</startdate><enddate>20100517</enddate><creator>Littler, Dene R.</creator><creator>Harrop, Stephen J.</creator><creator>Goodchild, Sophia C.</creator><creator>Phang, Juanita M.</creator><creator>Mynott, Andrew V.</creator><creator>Jiang, Lele</creator><creator>Valenzuela, Stella M.</creator><creator>Mazzanti, Michele</creator><creator>Brown, Louise J.</creator><creator>Breit, Samuel N.</creator><creator>Curmi, Paul M.G.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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><scope>7ST</scope><scope>C1K</scope><scope>SOI</scope></search><sort><creationdate>20100517</creationdate><title>The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?</title><author>Littler, Dene R. ; Harrop, Stephen J. ; Goodchild, Sophia C. ; Phang, Juanita M. ; Mynott, Andrew V. ; Jiang, Lele ; Valenzuela, Stella M. ; Mazzanti, Michele ; Brown, Louise J. ; Breit, Samuel N. ; Curmi, Paul M.G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5275-4a66e8f6cd37d29a83280720c3e9c594acabf8576fd8594eea2305f4a9907ef53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Cell Membrane - metabolism</topic><topic>Chloride Channels - chemistry</topic><topic>Chloride Channels - classification</topic><topic>Chloride Channels - genetics</topic><topic>Chloride Channels - metabolism</topic><topic>chloride intracellular channel</topic><topic>Chloride intracellular channel protein</topic><topic>Chordata</topic><topic>CLIC</topic><topic>CLIC1</topic><topic>Cytoskeleton - metabolism</topic><topic>dehydroascorbate reductase</topic><topic>DHAR</topic><topic>endoplasmic reticulum</topic><topic>Enzymes - chemistry</topic><topic>Enzymes - classification</topic><topic>Enzymes - genetics</topic><topic>Enzymes - metabolism</topic><topic>ERM</topic><topic>ezrin–moesin–radixin</topic><topic>glutaredoxin</topic><topic>glutathione</topic><topic>glutathione S-transferase</topic><topic>Grx</topic><topic>GSH</topic><topic>GST</topic><topic>GST omega</topic><topic>GSTO</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Membrane insertion</topic><topic>Metazoa</topic><topic>Oxidation-Reduction</topic><topic>Redox</topic><topic>transmembrane</topic><topic>Tubulogenesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Littler, Dene R.</creatorcontrib><creatorcontrib>Harrop, Stephen J.</creatorcontrib><creatorcontrib>Goodchild, Sophia C.</creatorcontrib><creatorcontrib>Phang, Juanita M.</creatorcontrib><creatorcontrib>Mynott, Andrew V.</creatorcontrib><creatorcontrib>Jiang, Lele</creatorcontrib><creatorcontrib>Valenzuela, Stella M.</creatorcontrib><creatorcontrib>Mazzanti, Michele</creatorcontrib><creatorcontrib>Brown, Louise J.</creatorcontrib><creatorcontrib>Breit, Samuel N.</creatorcontrib><creatorcontrib>Curmi, Paul M.G.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect: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><collection>Environment Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Environment Abstracts</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Littler, Dene R.</au><au>Harrop, Stephen J.</au><au>Goodchild, Sophia C.</au><au>Phang, Juanita M.</au><au>Mynott, Andrew V.</au><au>Jiang, Lele</au><au>Valenzuela, Stella M.</au><au>Mazzanti, Michele</au><au>Brown, Louise J.</au><au>Breit, Samuel N.</au><au>Curmi, Paul M.G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2010-05-17</date><risdate>2010</risdate><volume>584</volume><issue>10</issue><spage>2093</spage><epage>2101</epage><pages>2093-2101</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Chloride intracellular channel proteins (CLICs) are distinct from most ion channels in that they have both soluble and integral membrane forms. CLICs are highly conserved in chordates, with six vertebrate paralogues. CLIC-like proteins are found in other metazoans. CLICs form channels in artificial bilayers in a process favoured by oxidising conditions and low pH. They are structurally plastic, with CLIC1 adopting two distinct soluble conformations. Phylogenetic and structural data indicate that CLICs are likely to have enzymatic function. The physiological role of CLICs appears to be maintenance of intracellular membranes, which is associated with tubulogenesis but may involve other substructures.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>20085760</pmid><doi>10.1016/j.febslet.2010.01.027</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Cell Membrane - metabolism Chloride Channels - chemistry Chloride Channels - classification Chloride Channels - genetics Chloride Channels - metabolism chloride intracellular channel Chloride intracellular channel protein Chordata CLIC CLIC1 Cytoskeleton - metabolism dehydroascorbate reductase DHAR endoplasmic reticulum Enzymes - chemistry Enzymes - classification Enzymes - genetics Enzymes - metabolism ERM ezrin–moesin–radixin glutaredoxin glutathione glutathione S-transferase Grx GSH GST GST omega GSTO Humans Hydrogen-Ion Concentration Membrane insertion Metazoa Oxidation-Reduction Redox transmembrane Tubulogenesis |
| title | The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins? |
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