A Proteomic Study of Myosin II Motor Proteins during Tumor Cell Migration
Myosin II motor proteins play important roles in cell migration. Although myosin II filament assembly plays a key role in the stabilization of focal contacts at the leading edge of migrating cells, the mechanisms and signaling pathways regulating the localized assembly of lamellipodial myosin II fil...
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| Veröffentlicht in: | Journal of molecular biology 2011-04, Vol.407 (5), p.673-686 |
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| creator | Betapudi, Venkaiah Gokulrangan, Giridharan Chance, Mark R. Egelhoff, Thomas T. |
| description | Myosin II motor proteins play important roles in cell migration. Although myosin II filament assembly plays a key role in the stabilization of focal contacts at the leading edge of migrating cells, the mechanisms and signaling pathways regulating the localized assembly of lamellipodial myosin II filaments are poorly understood. We performed a proteomic analysis of myosin heavy chain (MHC) phosphorylation sites in MDA-MB 231 breast cancer cells to identify MHC phosphorylation sites that are activated during integrin engagement and lamellar extension on fibronectin. Fibronectin-activated MHC phosphorylation was identified on novel and previously recognized consensus sites for phosphorylation by protein kinase C and casein kinase II (CK-II). S1943, a CK-II consensus site, was highly phosphorylated in response to matrix engagement, and phosphoantibody staining revealed phosphorylation on myosin II assembled into leading-edge lamellae. Surprisingly, neither pharmacological reduction nor small inhibitory RNA reduction in CK-II activity reduced this stimulated S1943 phosphorylation. Our data demonstrate that S1943 phosphorylation is upregulated during lamellar protrusion, and that CK-II does not appear to be the kinase responsible for this matrix-induced phosphorylation event. |
| doi_str_mv | 10.1016/j.jmb.2011.02.010 |
| format | Article |
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Although myosin II filament assembly plays a key role in the stabilization of focal contacts at the leading edge of migrating cells, the mechanisms and signaling pathways regulating the localized assembly of lamellipodial myosin II filaments are poorly understood. We performed a proteomic analysis of myosin heavy chain (MHC) phosphorylation sites in MDA-MB 231 breast cancer cells to identify MHC phosphorylation sites that are activated during integrin engagement and lamellar extension on fibronectin. Fibronectin-activated MHC phosphorylation was identified on novel and previously recognized consensus sites for phosphorylation by protein kinase C and casein kinase II (CK-II). S1943, a CK-II consensus site, was highly phosphorylated in response to matrix engagement, and phosphoantibody staining revealed phosphorylation on myosin II assembled into leading-edge lamellae. Surprisingly, neither pharmacological reduction nor small inhibitory RNA reduction in CK-II activity reduced this stimulated S1943 phosphorylation. Our data demonstrate that S1943 phosphorylation is upregulated during lamellar protrusion, and that CK-II does not appear to be the kinase responsible for this matrix-induced phosphorylation event.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2011.02.010</identifier><identifier>PMID: 21316371</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>analysis ; Animals ; breast neoplasms ; Breast Neoplasms - metabolism ; Breast Neoplasms - pathology ; Casein Kinase II ; Casein Kinase II - chemistry ; Casein Kinase II - genetics ; Casein Kinase II - metabolism ; Cell Line, Tumor ; cell migration ; cell movement ; Cell Movement - physiology ; Cercopithecus aethiops ; chemistry ; Chlorocebus aethiops ; COS Cells ; cytoskeleton ; Female ; fibronectins ; Fibronectins - metabolism ; genetics ; HeLa Cells ; Humans ; integrins ; metabolism ; Models, Molecular ; myosin heavy chains ; Myosin Heavy Chains - chemistry ; Myosin Heavy Chains - genetics ; Myosin Heavy Chains - metabolism ; myosin II ; Myosin Type II ; Myosin Type II - chemistry ; Myosin Type II - genetics ; Myosin Type II - metabolism ; pathology ; Phosphorylation ; physiology ; Protein Isoforms ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; protein kinase C ; protein phosphorylation ; Proteome ; Proteome - analysis ; proteomics ; Pseudopodia ; Pseudopodia - metabolism ; Recombinant Fusion Proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; RNA ; RNA, Small Interfering ; RNA, Small Interfering - genetics ; RNA, Small Interfering - metabolism ; signal transduction</subject><ispartof>Journal of molecular biology, 2011-04, Vol.407 (5), p.673-686</ispartof><rights>2011 Elsevier Ltd</rights><rights>Copyright © 2011 Elsevier Ltd. All rights reserved.</rights><rights>2011 Elsevier Ltd. All rights reserved. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c507t-e82845eba117a733e20ae15e196ec03095c8eec26d559c0735b95b3a565444dc3</citedby><cites>FETCH-LOGICAL-c507t-e82845eba117a733e20ae15e196ec03095c8eec26d559c0735b95b3a565444dc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022283611001434$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21316371$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Betapudi, Venkaiah</creatorcontrib><creatorcontrib>Gokulrangan, Giridharan</creatorcontrib><creatorcontrib>Chance, Mark R.</creatorcontrib><creatorcontrib>Egelhoff, Thomas T.</creatorcontrib><title>A Proteomic Study of Myosin II Motor Proteins during Tumor Cell Migration</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Myosin II motor proteins play important roles in cell migration. Although myosin II filament assembly plays a key role in the stabilization of focal contacts at the leading edge of migrating cells, the mechanisms and signaling pathways regulating the localized assembly of lamellipodial myosin II filaments are poorly understood. We performed a proteomic analysis of myosin heavy chain (MHC) phosphorylation sites in MDA-MB 231 breast cancer cells to identify MHC phosphorylation sites that are activated during integrin engagement and lamellar extension on fibronectin. Fibronectin-activated MHC phosphorylation was identified on novel and previously recognized consensus sites for phosphorylation by protein kinase C and casein kinase II (CK-II). S1943, a CK-II consensus site, was highly phosphorylated in response to matrix engagement, and phosphoantibody staining revealed phosphorylation on myosin II assembled into leading-edge lamellae. Surprisingly, neither pharmacological reduction nor small inhibitory RNA reduction in CK-II activity reduced this stimulated S1943 phosphorylation. Our data demonstrate that S1943 phosphorylation is upregulated during lamellar protrusion, and that CK-II does not appear to be the kinase responsible for this matrix-induced phosphorylation event.</description><subject>analysis</subject><subject>Animals</subject><subject>breast neoplasms</subject><subject>Breast Neoplasms - metabolism</subject><subject>Breast Neoplasms - pathology</subject><subject>Casein Kinase II</subject><subject>Casein Kinase II - chemistry</subject><subject>Casein Kinase II - genetics</subject><subject>Casein Kinase II - metabolism</subject><subject>Cell Line, Tumor</subject><subject>cell migration</subject><subject>cell movement</subject><subject>Cell Movement - physiology</subject><subject>Cercopithecus aethiops</subject><subject>chemistry</subject><subject>Chlorocebus aethiops</subject><subject>COS Cells</subject><subject>cytoskeleton</subject><subject>Female</subject><subject>fibronectins</subject><subject>Fibronectins - metabolism</subject><subject>genetics</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>integrins</subject><subject>metabolism</subject><subject>Models, Molecular</subject><subject>myosin heavy chains</subject><subject>Myosin Heavy Chains - chemistry</subject><subject>Myosin Heavy Chains - genetics</subject><subject>Myosin Heavy Chains - metabolism</subject><subject>myosin II</subject><subject>Myosin Type II</subject><subject>Myosin Type II - chemistry</subject><subject>Myosin Type II - genetics</subject><subject>Myosin Type II - metabolism</subject><subject>pathology</subject><subject>Phosphorylation</subject><subject>physiology</subject><subject>Protein Isoforms</subject><subject>Protein Isoforms - chemistry</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>protein kinase C</subject><subject>protein phosphorylation</subject><subject>Proteome</subject><subject>Proteome - analysis</subject><subject>proteomics</subject><subject>Pseudopodia</subject><subject>Pseudopodia - metabolism</subject><subject>Recombinant Fusion Proteins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RNA</subject><subject>RNA, Small Interfering</subject><subject>RNA, Small Interfering - genetics</subject><subject>RNA, Small Interfering - metabolism</subject><subject>signal transduction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kdFqFDEUhoModq0-gDeaO72Z8SSZZDIIQlmqLnRpoe11yGTOrll2JjWZKezbN-vUoje9CiTf-flPPkLeMygZMPVlV-76tuTAWAm8BAYvyIKBbgqthH5JFgCcF1wLdULepLQDACkq_ZqccCaYEjVbkNUZvYphxNB7R6_HqTvQsKHrQ0h-oKsVXYcxxBnxQ6LdFP2wpTdTn2-XuN_Ttd9GO_owvCWvNnaf8N3jeUpuv5_fLH8WF5c_Vsuzi8JJqMcCNdeVxNYyVttaCORgkUlkjUIHAhrpNKLjqpOycVAL2TayFVYqWVVV58Qp-Tbn3k1tj53DYYx2b-6i7208mGC9-f9l8L_MNtwbATWvQeeAT48BMfyeMI2m98nlXeyAYUpGyz8VG5XJz8-STNU8hzZNk1E2oy6GlCJungoxMEdZZmeyLHOUZYCbLCvPfPh3k6eJv3Yy8HEGNjYYu40-mdvrnCCzyUpJcYz4OhOYf_zeYzTJeRwcdj6iG00X_DMFHgCJw60t</recordid><startdate>20110415</startdate><enddate>20110415</enddate><creator>Betapudi, Venkaiah</creator><creator>Gokulrangan, Giridharan</creator><creator>Chance, Mark R.</creator><creator>Egelhoff, Thomas T.</creator><general>Elsevier Ltd</general><scope>FBQ</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>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110415</creationdate><title>A Proteomic Study of Myosin II Motor Proteins during Tumor Cell Migration</title><author>Betapudi, Venkaiah ; Gokulrangan, Giridharan ; Chance, Mark R. ; Egelhoff, Thomas T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c507t-e82845eba117a733e20ae15e196ec03095c8eec26d559c0735b95b3a565444dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>analysis</topic><topic>Animals</topic><topic>breast neoplasms</topic><topic>Breast Neoplasms - metabolism</topic><topic>Breast Neoplasms - pathology</topic><topic>Casein Kinase II</topic><topic>Casein Kinase II - chemistry</topic><topic>Casein Kinase II - genetics</topic><topic>Casein Kinase II - metabolism</topic><topic>Cell Line, Tumor</topic><topic>cell migration</topic><topic>cell movement</topic><topic>Cell Movement - physiology</topic><topic>Cercopithecus aethiops</topic><topic>chemistry</topic><topic>Chlorocebus aethiops</topic><topic>COS Cells</topic><topic>cytoskeleton</topic><topic>Female</topic><topic>fibronectins</topic><topic>Fibronectins - metabolism</topic><topic>genetics</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>integrins</topic><topic>metabolism</topic><topic>Models, Molecular</topic><topic>myosin heavy chains</topic><topic>Myosin Heavy Chains - chemistry</topic><topic>Myosin Heavy Chains - genetics</topic><topic>Myosin Heavy Chains - metabolism</topic><topic>myosin II</topic><topic>Myosin Type II</topic><topic>Myosin Type II - chemistry</topic><topic>Myosin Type II - genetics</topic><topic>Myosin Type II - metabolism</topic><topic>pathology</topic><topic>Phosphorylation</topic><topic>physiology</topic><topic>Protein Isoforms</topic><topic>Protein Isoforms - chemistry</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>protein kinase C</topic><topic>protein phosphorylation</topic><topic>Proteome</topic><topic>Proteome - analysis</topic><topic>proteomics</topic><topic>Pseudopodia</topic><topic>Pseudopodia - metabolism</topic><topic>Recombinant Fusion Proteins</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RNA</topic><topic>RNA, Small Interfering</topic><topic>RNA, Small Interfering - genetics</topic><topic>RNA, Small Interfering - metabolism</topic><topic>signal transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Betapudi, Venkaiah</creatorcontrib><creatorcontrib>Gokulrangan, Giridharan</creatorcontrib><creatorcontrib>Chance, Mark R.</creatorcontrib><creatorcontrib>Egelhoff, Thomas T.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Betapudi, Venkaiah</au><au>Gokulrangan, Giridharan</au><au>Chance, Mark R.</au><au>Egelhoff, Thomas T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Proteomic Study of Myosin II Motor Proteins during Tumor Cell Migration</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2011-04-15</date><risdate>2011</risdate><volume>407</volume><issue>5</issue><spage>673</spage><epage>686</epage><pages>673-686</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>Myosin II motor proteins play important roles in cell migration. Although myosin II filament assembly plays a key role in the stabilization of focal contacts at the leading edge of migrating cells, the mechanisms and signaling pathways regulating the localized assembly of lamellipodial myosin II filaments are poorly understood. We performed a proteomic analysis of myosin heavy chain (MHC) phosphorylation sites in MDA-MB 231 breast cancer cells to identify MHC phosphorylation sites that are activated during integrin engagement and lamellar extension on fibronectin. Fibronectin-activated MHC phosphorylation was identified on novel and previously recognized consensus sites for phosphorylation by protein kinase C and casein kinase II (CK-II). S1943, a CK-II consensus site, was highly phosphorylated in response to matrix engagement, and phosphoantibody staining revealed phosphorylation on myosin II assembled into leading-edge lamellae. Surprisingly, neither pharmacological reduction nor small inhibitory RNA reduction in CK-II activity reduced this stimulated S1943 phosphorylation. Our data demonstrate that S1943 phosphorylation is upregulated during lamellar protrusion, and that CK-II does not appear to be the kinase responsible for this matrix-induced phosphorylation event.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>21316371</pmid><doi>10.1016/j.jmb.2011.02.010</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | analysis Animals breast neoplasms Breast Neoplasms - metabolism Breast Neoplasms - pathology Casein Kinase II Casein Kinase II - chemistry Casein Kinase II - genetics Casein Kinase II - metabolism Cell Line, Tumor cell migration cell movement Cell Movement - physiology Cercopithecus aethiops chemistry Chlorocebus aethiops COS Cells cytoskeleton Female fibronectins Fibronectins - metabolism genetics HeLa Cells Humans integrins metabolism Models, Molecular myosin heavy chains Myosin Heavy Chains - chemistry Myosin Heavy Chains - genetics Myosin Heavy Chains - metabolism myosin II Myosin Type II Myosin Type II - chemistry Myosin Type II - genetics Myosin Type II - metabolism pathology Phosphorylation physiology Protein Isoforms Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism protein kinase C protein phosphorylation Proteome Proteome - analysis proteomics Pseudopodia Pseudopodia - metabolism Recombinant Fusion Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA RNA, Small Interfering RNA, Small Interfering - genetics RNA, Small Interfering - metabolism signal transduction |
| title | A Proteomic Study of Myosin II Motor Proteins during Tumor Cell Migration |
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