Annexin A6-A multifunctional scaffold in cell motility
Annexin A6 (AnxA6) belongs to a highly conserved protein family characterized by their calcium (Ca 2+ )-dependent binding to phospholipids. Over the years, immunohistochemistry, subcellular fractionations, and live cell microscopy established that AnxA6 is predominantly found at the plasma membrane...
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| Veröffentlicht in: | Cell adhesion & migration 2017-05, Vol.11 (3), p.288-304 |
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| container_title | Cell adhesion & migration |
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| creator | Grewal, Thomas Hoque, Monira Conway, James R. W. Reverter, Meritxell Wahba, Mohamed Beevi, Syed S. Timpson, Paul Enrich, Carlos Rentero, Carles |
| description | Annexin A6 (AnxA6) belongs to a highly conserved protein family characterized by their calcium (Ca
2+
)-dependent binding to phospholipids. Over the years, immunohistochemistry, subcellular fractionations, and live cell microscopy established that AnxA6 is predominantly found at the plasma membrane and endosomal compartments. In these locations, AnxA6 acts as a multifunctional scaffold protein, recruiting signaling proteins, modulating cholesterol and membrane transport and influencing actin dynamics. These activities enable AnxA6 to contribute to the formation of multifactorial protein complexes and membrane domains relevant in signal transduction, cholesterol homeostasis and endo-/exocytic membrane transport. Hence, AnxA6 has been implicated in many biological processes, including cell proliferation, survival, differentiation, inflammation, but also membrane repair and viral infection. More recently, we and others identified roles for AnxA6 in cancer cell migration and invasion. This review will discuss how the multiple scaffold functions may enable AnxA6 to modulate migratory cell behavior in health and disease. |
| doi_str_mv | 10.1080/19336918.2016.1268318 |
| format | Article |
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2+
)-dependent binding to phospholipids. Over the years, immunohistochemistry, subcellular fractionations, and live cell microscopy established that AnxA6 is predominantly found at the plasma membrane and endosomal compartments. In these locations, AnxA6 acts as a multifunctional scaffold protein, recruiting signaling proteins, modulating cholesterol and membrane transport and influencing actin dynamics. These activities enable AnxA6 to contribute to the formation of multifactorial protein complexes and membrane domains relevant in signal transduction, cholesterol homeostasis and endo-/exocytic membrane transport. Hence, AnxA6 has been implicated in many biological processes, including cell proliferation, survival, differentiation, inflammation, but also membrane repair and viral infection. More recently, we and others identified roles for AnxA6 in cancer cell migration and invasion. This review will discuss how the multiple scaffold functions may enable AnxA6 to modulate migratory cell behavior in health and disease.</description><identifier>ISSN: 1933-6918</identifier><identifier>EISSN: 1933-6926</identifier><identifier>DOI: 10.1080/19336918.2016.1268318</identifier><identifier>PMID: 28060548</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>actin ; Annexin A6 ; caveolin ; cholesterol ; EGFR/Ras ; integrins ; invasion ; migration ; p120GAP ; PKCα ; Review ; scaffold ; SNAREs</subject><ispartof>Cell adhesion & migration, 2017-05, Vol.11 (3), p.288-304</ispartof><rights>2017 Taylor & Francis 2017</rights><rights>2017 Taylor & Francis 2017 Taylor & Francis</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3838-9514a976307a84651f6c9c2797ceef82973ceb7aad85250d9685e2d49b8814833</citedby><cites>FETCH-LOGICAL-c3838-9514a976307a84651f6c9c2797ceef82973ceb7aad85250d9685e2d49b8814833</cites><orcidid>0000-0003-0382-2993</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5479450/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5479450/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28060548$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Grewal, Thomas</creatorcontrib><creatorcontrib>Hoque, Monira</creatorcontrib><creatorcontrib>Conway, James R. W.</creatorcontrib><creatorcontrib>Reverter, Meritxell</creatorcontrib><creatorcontrib>Wahba, Mohamed</creatorcontrib><creatorcontrib>Beevi, Syed S.</creatorcontrib><creatorcontrib>Timpson, Paul</creatorcontrib><creatorcontrib>Enrich, Carlos</creatorcontrib><creatorcontrib>Rentero, Carles</creatorcontrib><title>Annexin A6-A multifunctional scaffold in cell motility</title><title>Cell adhesion & migration</title><addtitle>Cell Adh Migr</addtitle><description>Annexin A6 (AnxA6) belongs to a highly conserved protein family characterized by their calcium (Ca
2+
)-dependent binding to phospholipids. Over the years, immunohistochemistry, subcellular fractionations, and live cell microscopy established that AnxA6 is predominantly found at the plasma membrane and endosomal compartments. In these locations, AnxA6 acts as a multifunctional scaffold protein, recruiting signaling proteins, modulating cholesterol and membrane transport and influencing actin dynamics. These activities enable AnxA6 to contribute to the formation of multifactorial protein complexes and membrane domains relevant in signal transduction, cholesterol homeostasis and endo-/exocytic membrane transport. Hence, AnxA6 has been implicated in many biological processes, including cell proliferation, survival, differentiation, inflammation, but also membrane repair and viral infection. More recently, we and others identified roles for AnxA6 in cancer cell migration and invasion. This review will discuss how the multiple scaffold functions may enable AnxA6 to modulate migratory cell behavior in health and disease.</description><subject>actin</subject><subject>Annexin A6</subject><subject>caveolin</subject><subject>cholesterol</subject><subject>EGFR/Ras</subject><subject>integrins</subject><subject>invasion</subject><subject>migration</subject><subject>p120GAP</subject><subject>PKCα</subject><subject>Review</subject><subject>scaffold</subject><subject>SNAREs</subject><issn>1933-6918</issn><issn>1933-6926</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNp9kE1PxCAQhonR-P0TND166Qql0OFi3Gz8Sky86JmwFBRDQaFV99_bza4bvXhiAs-8wzwInRA8IRjwORGUckFgUmHCJ6TiQAlsof3lfclFxbc3NYE9dJDzK8YMCOe7aK8CzDGrYR_xaQjmy4Viystp0Q2-d3YIuncxKF9krayNvi1GQBvviy72zrt-cYR2rPLZHK_PQ_R0ffU4uy3vH27uZtP7UlOgUApGaiUaTnGjoOaMWK6FrhrRaGMsVKKh2swbpVpgFcOt4MBM1dZiDkBqoPQQXaxy34Z5Z1ptQp-Ul2_JdSotZFRO_n0J7kU-xw_J6kbUDI8BZ-uAFN8Hk3vZubxcRQUThywJMM4EJqQZUbZCdYo5J2M3YwiWS-fyx7lcOpdr52Pf6e8_brp-JI_A5QpwwcbUqc-YfCt7tfAx2aSCdlnS_2d8A7Cyj9M</recordid><startdate>20170504</startdate><enddate>20170504</enddate><creator>Grewal, Thomas</creator><creator>Hoque, Monira</creator><creator>Conway, James R. W.</creator><creator>Reverter, Meritxell</creator><creator>Wahba, Mohamed</creator><creator>Beevi, Syed S.</creator><creator>Timpson, Paul</creator><creator>Enrich, Carlos</creator><creator>Rentero, Carles</creator><general>Taylor & Francis</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-0382-2993</orcidid></search><sort><creationdate>20170504</creationdate><title>Annexin A6-A multifunctional scaffold in cell motility</title><author>Grewal, Thomas ; Hoque, Monira ; Conway, James R. W. ; Reverter, Meritxell ; Wahba, Mohamed ; Beevi, Syed S. ; Timpson, Paul ; Enrich, Carlos ; Rentero, Carles</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3838-9514a976307a84651f6c9c2797ceef82973ceb7aad85250d9685e2d49b8814833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>actin</topic><topic>Annexin A6</topic><topic>caveolin</topic><topic>cholesterol</topic><topic>EGFR/Ras</topic><topic>integrins</topic><topic>invasion</topic><topic>migration</topic><topic>p120GAP</topic><topic>PKCα</topic><topic>Review</topic><topic>scaffold</topic><topic>SNAREs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Grewal, Thomas</creatorcontrib><creatorcontrib>Hoque, Monira</creatorcontrib><creatorcontrib>Conway, James R. W.</creatorcontrib><creatorcontrib>Reverter, Meritxell</creatorcontrib><creatorcontrib>Wahba, Mohamed</creatorcontrib><creatorcontrib>Beevi, Syed S.</creatorcontrib><creatorcontrib>Timpson, Paul</creatorcontrib><creatorcontrib>Enrich, Carlos</creatorcontrib><creatorcontrib>Rentero, Carles</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell adhesion & migration</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Grewal, Thomas</au><au>Hoque, Monira</au><au>Conway, James R. W.</au><au>Reverter, Meritxell</au><au>Wahba, Mohamed</au><au>Beevi, Syed S.</au><au>Timpson, Paul</au><au>Enrich, Carlos</au><au>Rentero, Carles</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Annexin A6-A multifunctional scaffold in cell motility</atitle><jtitle>Cell adhesion & migration</jtitle><addtitle>Cell Adh Migr</addtitle><date>2017-05-04</date><risdate>2017</risdate><volume>11</volume><issue>3</issue><spage>288</spage><epage>304</epage><pages>288-304</pages><issn>1933-6918</issn><eissn>1933-6926</eissn><abstract>Annexin A6 (AnxA6) belongs to a highly conserved protein family characterized by their calcium (Ca
2+
)-dependent binding to phospholipids. Over the years, immunohistochemistry, subcellular fractionations, and live cell microscopy established that AnxA6 is predominantly found at the plasma membrane and endosomal compartments. In these locations, AnxA6 acts as a multifunctional scaffold protein, recruiting signaling proteins, modulating cholesterol and membrane transport and influencing actin dynamics. These activities enable AnxA6 to contribute to the formation of multifactorial protein complexes and membrane domains relevant in signal transduction, cholesterol homeostasis and endo-/exocytic membrane transport. Hence, AnxA6 has been implicated in many biological processes, including cell proliferation, survival, differentiation, inflammation, but also membrane repair and viral infection. More recently, we and others identified roles for AnxA6 in cancer cell migration and invasion. This review will discuss how the multiple scaffold functions may enable AnxA6 to modulate migratory cell behavior in health and disease.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>28060548</pmid><doi>10.1080/19336918.2016.1268318</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0003-0382-2993</orcidid><oa>free_for_read</oa></addata></record> |
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| source | EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | actin Annexin A6 caveolin cholesterol EGFR/Ras integrins invasion migration p120GAP PKCα Review scaffold SNAREs |
| title | Annexin A6-A multifunctional scaffold in cell motility |
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