Integrin CD11c/CD18 α-Chain Phosphorylation Is Functionally Important
CD11c/CD18 (αXβ2, p150/95, or complement receptor 4, CR4) is a monocyte/macrophage-enriched integrin that has been reported to bind to a variety of ligands. These include cell surface proteins, extracellular matrix proteins, and soluble ligands. The regulation of ligand binding to CD11c/CD18 has rem...
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| Veröffentlicht in: | The Journal of biological chemistry 2013-11, Vol.288 (46), p.33494-33499 |
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| container_title | The Journal of biological chemistry |
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| creator | Uotila, Liisa M. Aatonen, Maria Gahmberg, Carl G. |
| description | CD11c/CD18 (αXβ2, p150/95, or complement receptor 4, CR4) is a monocyte/macrophage-enriched integrin that has been reported to bind to a variety of ligands. These include cell surface proteins, extracellular matrix proteins, and soluble ligands. The regulation of ligand binding to CD11c/CD18 has remained poorly understood. Previous work has shown that both α-chain and β-chain phosphorylations of CD11a/CD18 and CD11b/CD18 are needed for activity, but no corresponding studies on CD11c/CD18 have been performed. In this study, we have identified the phosphorylation site of CD11c as Ser-1158 and show that it is pivotal for adherence and phagocytosis.
Background: Leukocyte integrins are involved in cell adhesion, cell migration, and phagocytosis.
Results: CD11c/CD18, a leukocyte integrin expressed on monocytes, macrophages, and dendritic cells, is phosphorylated on Ser-1158 of the α-chain. Abrogation of phosphorylation results in impaired adhesion and phagocytosis.
Conclusion: Integrin inside-out activated adhesion is regulated by a single phosphorylation site on CD11c.
Significance: Regulation of integrin activity is essential for immune cells. |
| doi_str_mv | 10.1074/jbc.C113.497446 |
| format | Article |
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Background: Leukocyte integrins are involved in cell adhesion, cell migration, and phagocytosis.
Results: CD11c/CD18, a leukocyte integrin expressed on monocytes, macrophages, and dendritic cells, is phosphorylated on Ser-1158 of the α-chain. Abrogation of phosphorylation results in impaired adhesion and phagocytosis.
Conclusion: Integrin inside-out activated adhesion is regulated by a single phosphorylation site on CD11c.
Significance: Regulation of integrin activity is essential for immune cells.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.C113.497446</identifier><identifier>PMID: 24129562</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adhesion ; Animals ; CD11c Antigen - genetics ; CD11c Antigen - metabolism ; CD18 Antigens - genetics ; CD18 Antigens - metabolism ; Cell Adhesion - physiology ; Chlorocebus aethiops ; COS Cells ; Humans ; Integrins ; K562 Cells ; Leukocyte ; Phagocytosis ; Phagocytosis - physiology ; Phosphorylation ; Phosphorylation - physiology</subject><ispartof>The Journal of biological chemistry, 2013-11, Vol.288 (46), p.33494-33499</ispartof><rights>2013 © 2013 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-4468fdb5130cef95b8b0bc4b2aa238581081faaaf0addd44aad14252517bd4dd3</citedby><cites>FETCH-LOGICAL-c443t-4468fdb5130cef95b8b0bc4b2aa238581081faaaf0addd44aad14252517bd4dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3829194/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3829194/$$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/24129562$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Uotila, Liisa M.</creatorcontrib><creatorcontrib>Aatonen, Maria</creatorcontrib><creatorcontrib>Gahmberg, Carl G.</creatorcontrib><title>Integrin CD11c/CD18 α-Chain Phosphorylation Is Functionally Important</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>CD11c/CD18 (αXβ2, p150/95, or complement receptor 4, CR4) is a monocyte/macrophage-enriched integrin that has been reported to bind to a variety of ligands. These include cell surface proteins, extracellular matrix proteins, and soluble ligands. The regulation of ligand binding to CD11c/CD18 has remained poorly understood. Previous work has shown that both α-chain and β-chain phosphorylations of CD11a/CD18 and CD11b/CD18 are needed for activity, but no corresponding studies on CD11c/CD18 have been performed. In this study, we have identified the phosphorylation site of CD11c as Ser-1158 and show that it is pivotal for adherence and phagocytosis.
Background: Leukocyte integrins are involved in cell adhesion, cell migration, and phagocytosis.
Results: CD11c/CD18, a leukocyte integrin expressed on monocytes, macrophages, and dendritic cells, is phosphorylated on Ser-1158 of the α-chain. Abrogation of phosphorylation results in impaired adhesion and phagocytosis.
Conclusion: Integrin inside-out activated adhesion is regulated by a single phosphorylation site on CD11c.
Significance: Regulation of integrin activity is essential for immune cells.</description><subject>Adhesion</subject><subject>Animals</subject><subject>CD11c Antigen - genetics</subject><subject>CD11c Antigen - metabolism</subject><subject>CD18 Antigens - genetics</subject><subject>CD18 Antigens - metabolism</subject><subject>Cell Adhesion - physiology</subject><subject>Chlorocebus aethiops</subject><subject>COS Cells</subject><subject>Humans</subject><subject>Integrins</subject><subject>K562 Cells</subject><subject>Leukocyte</subject><subject>Phagocytosis</subject><subject>Phagocytosis - physiology</subject><subject>Phosphorylation</subject><subject>Phosphorylation - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEFPIyEYhslmzbZWz97MHPcyLR8D7czFxIxWm5jowU32Rr4BxtJMocLUpD_LP7K_aWmqjXtYDkDg4eXNQ8gF0DHQGZ-sGjWuAYoxr2acT7-RIdCyyAsBv7-TIaUM8oqJckBOY1zRNHgFP8iAcWCVmLIhmS9cb16CdVl9A6AmaS6zP-95vcR09rT0cbP0Yddhb73LFjGbb53a77HrdtlivfGhR9efkZMWu2jOP9YR-TW_fa7v84fHu0V9_ZArzos-TxXLVjcCCqpMW4mmbGijeMMQWVGKMpWHFhFbilprzhE1cCaYgFmjudbFiFwdcjfbZm20Mq4P2MlNsGsMO-nRyn9vnF3KF_8mi5JVUPEU8PMjIPjXrYm9XNuoTNehM34bJXCRxIgpZwmdHFAVfIzBtMdvgMq9fZnsy719ebCfXlx-bXfkP3UnoDoAJjl6sybIqKxxymgbjOql9va_4X8B8ySVFw</recordid><startdate>20131115</startdate><enddate>20131115</enddate><creator>Uotila, Liisa M.</creator><creator>Aatonen, Maria</creator><creator>Gahmberg, Carl G.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>5PM</scope></search><sort><creationdate>20131115</creationdate><title>Integrin CD11c/CD18 α-Chain Phosphorylation Is Functionally Important</title><author>Uotila, Liisa M. ; Aatonen, Maria ; Gahmberg, Carl G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-4468fdb5130cef95b8b0bc4b2aa238581081faaaf0addd44aad14252517bd4dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adhesion</topic><topic>Animals</topic><topic>CD11c Antigen - genetics</topic><topic>CD11c Antigen - metabolism</topic><topic>CD18 Antigens - genetics</topic><topic>CD18 Antigens - metabolism</topic><topic>Cell Adhesion - physiology</topic><topic>Chlorocebus aethiops</topic><topic>COS Cells</topic><topic>Humans</topic><topic>Integrins</topic><topic>K562 Cells</topic><topic>Leukocyte</topic><topic>Phagocytosis</topic><topic>Phagocytosis - physiology</topic><topic>Phosphorylation</topic><topic>Phosphorylation - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Uotila, Liisa M.</creatorcontrib><creatorcontrib>Aatonen, Maria</creatorcontrib><creatorcontrib>Gahmberg, Carl 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>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Uotila, Liisa M.</au><au>Aatonen, Maria</au><au>Gahmberg, Carl G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Integrin CD11c/CD18 α-Chain Phosphorylation Is Functionally Important</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2013-11-15</date><risdate>2013</risdate><volume>288</volume><issue>46</issue><spage>33494</spage><epage>33499</epage><pages>33494-33499</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>CD11c/CD18 (αXβ2, p150/95, or complement receptor 4, CR4) is a monocyte/macrophage-enriched integrin that has been reported to bind to a variety of ligands. These include cell surface proteins, extracellular matrix proteins, and soluble ligands. The regulation of ligand binding to CD11c/CD18 has remained poorly understood. Previous work has shown that both α-chain and β-chain phosphorylations of CD11a/CD18 and CD11b/CD18 are needed for activity, but no corresponding studies on CD11c/CD18 have been performed. In this study, we have identified the phosphorylation site of CD11c as Ser-1158 and show that it is pivotal for adherence and phagocytosis.
Background: Leukocyte integrins are involved in cell adhesion, cell migration, and phagocytosis.
Results: CD11c/CD18, a leukocyte integrin expressed on monocytes, macrophages, and dendritic cells, is phosphorylated on Ser-1158 of the α-chain. Abrogation of phosphorylation results in impaired adhesion and phagocytosis.
Conclusion: Integrin inside-out activated adhesion is regulated by a single phosphorylation site on CD11c.
Significance: Regulation of integrin activity is essential for immune cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>24129562</pmid><doi>10.1074/jbc.C113.497446</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| subjects | Adhesion Animals CD11c Antigen - genetics CD11c Antigen - metabolism CD18 Antigens - genetics CD18 Antigens - metabolism Cell Adhesion - physiology Chlorocebus aethiops COS Cells Humans Integrins K562 Cells Leukocyte Phagocytosis Phagocytosis - physiology Phosphorylation Phosphorylation - physiology |
| title | Integrin CD11c/CD18 α-Chain Phosphorylation Is Functionally Important |
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