PDZ Domains and Viral Infection: Versatile Potentials of HPV-PDZ Interactions in relation to Malignancy
Cervical cancer is caused by high-risk human papillomaviruses (HPVs), and a unique characteristic of these is a PDZ (P̲SD-95/D̲lg/Z̲O-1-)binding motif in their E6 proteins. Through this motif HPV E6 interacts with a variety of PDZ domain-containing proteins and targets them mainly for degradation. T...
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| description | Cervical cancer is caused by high-risk human papillomaviruses (HPVs), and a unique characteristic of these is a PDZ (P̲SD-95/D̲lg/Z̲O-1-)binding motif in their E6 proteins. Through this motif HPV E6 interacts with a variety of PDZ domain-containing proteins and targets them mainly for degradation. These E6-PDZ interactions exhibit extraordinarily different functions in relation to HPV-induced malignancy, depending upon various cellular contexts; for example, Dlg and Scrib show different distribution patterns from what is seen in normal epithelium, both in localization and in amount, and their loss may be a late-stage marker in malignant progression. Recent studies show that interactions with specific forms of the proteins may have oncogenic potential. In addition, it is interesting that PDZ proteins make a contribution to the stabilization of E6 and viral episomal maintenance during the course of HPV life cycle. Various posttranslational modifications also greatly affect their functions. Phosphorylation of hDlg and hScrib by certain kinases regulates several important signaling cascades, and E6-PDZ interactions themselves are regulated through PKA-dependent phosphorylation. Thus these interactions naturally have great potential for both predictive and therapeutic applications, and, with development of screening tools for identifying novel targets of their interactions, comprehensive spatiotemporal analysis is currently underway. |
| doi_str_mv | 10.1155/2013/369712 |
| format | Article |
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Through this motif HPV E6 interacts with a variety of PDZ domain-containing proteins and targets them mainly for degradation. These E6-PDZ interactions exhibit extraordinarily different functions in relation to HPV-induced malignancy, depending upon various cellular contexts; for example, Dlg and Scrib show different distribution patterns from what is seen in normal epithelium, both in localization and in amount, and their loss may be a late-stage marker in malignant progression. Recent studies show that interactions with specific forms of the proteins may have oncogenic potential. In addition, it is interesting that PDZ proteins make a contribution to the stabilization of E6 and viral episomal maintenance during the course of HPV life cycle. Various posttranslational modifications also greatly affect their functions. Phosphorylation of hDlg and hScrib by certain kinases regulates several important signaling cascades, and E6-PDZ interactions themselves are regulated through PKA-dependent phosphorylation. Thus these interactions naturally have great potential for both predictive and therapeutic applications, and, with development of screening tools for identifying novel targets of their interactions, comprehensive spatiotemporal analysis is currently underway.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2013/369712</identifier><identifier>PMID: 24093094</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Amino Acid Sequence ; Causes of ; Cell cycle ; Cervical cancer ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Female ; Health aspects ; Human papillomavirus ; Humans ; Kinases ; Membrane Proteins - metabolism ; Oncogene Proteins, Viral - chemistry ; Oncogene Proteins, Viral - genetics ; Oncogene Proteins, Viral - metabolism ; Papillomavirus Infections - complications ; Papillomavirus Infections - genetics ; Papillomavirus Infections - metabolism ; Papillomaviruses ; PDZ Domains - genetics ; Phosphorylation ; Protein Binding ; Protein Interaction Domains and Motifs - genetics ; Repressor Proteins - chemistry ; Repressor Proteins - genetics ; Repressor Proteins - metabolism ; Review ; Tumors ; Uterine Cervical Neoplasms - complications ; Uterine Cervical Neoplasms - genetics ; Uterine Cervical Neoplasms - virology</subject><ispartof>BioMed research international, 2013-01, Vol.2013 (2013), p.1-9</ispartof><rights>Copyright © 2013 Kazunori Nagasaka et al.</rights><rights>COPYRIGHT 2013 John Wiley & Sons, Inc.</rights><rights>Copyright © 2013 Kazunori Nagasaka et al. Kazunori Nagasaka et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2013 Kazunori Nagasaka et al. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c594t-1d32c4f6ed7641752455332130e5e26e64fcbd077be32cd2735cfd7afa9a0b4e3</citedby><cites>FETCH-LOGICAL-c594t-1d32c4f6ed7641752455332130e5e26e64fcbd077be32cd2735cfd7afa9a0b4e3</cites><orcidid>0000-0002-0696-5175</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/PMC3777178/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3777178/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24093094$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Cantin, Edouard</contributor><creatorcontrib>Fujii, Tomoyuki</creatorcontrib><creatorcontrib>Osuga, Yutaka</creatorcontrib><creatorcontrib>Kawana, Kei</creatorcontrib><creatorcontrib>Nagasaka, Kazunori</creatorcontrib><title>PDZ Domains and Viral Infection: Versatile Potentials of HPV-PDZ Interactions in relation to Malignancy</title><title>BioMed research international</title><addtitle>Biomed Res Int</addtitle><description>Cervical cancer is caused by high-risk human papillomaviruses (HPVs), and a unique characteristic of these is a PDZ (P̲SD-95/D̲lg/Z̲O-1-)binding motif in their E6 proteins. Through this motif HPV E6 interacts with a variety of PDZ domain-containing proteins and targets them mainly for degradation. These E6-PDZ interactions exhibit extraordinarily different functions in relation to HPV-induced malignancy, depending upon various cellular contexts; for example, Dlg and Scrib show different distribution patterns from what is seen in normal epithelium, both in localization and in amount, and their loss may be a late-stage marker in malignant progression. Recent studies show that interactions with specific forms of the proteins may have oncogenic potential. In addition, it is interesting that PDZ proteins make a contribution to the stabilization of E6 and viral episomal maintenance during the course of HPV life cycle. Various posttranslational modifications also greatly affect their functions. Phosphorylation of hDlg and hScrib by certain kinases regulates several important signaling cascades, and E6-PDZ interactions themselves are regulated through PKA-dependent phosphorylation. Thus these interactions naturally have great potential for both predictive and therapeutic applications, and, with development of screening tools for identifying novel targets of their interactions, comprehensive spatiotemporal analysis is currently underway.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Causes of</subject><subject>Cell cycle</subject><subject>Cervical cancer</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Female</subject><subject>Health aspects</subject><subject>Human papillomavirus</subject><subject>Humans</subject><subject>Kinases</subject><subject>Membrane Proteins - metabolism</subject><subject>Oncogene Proteins, Viral - chemistry</subject><subject>Oncogene Proteins, Viral - genetics</subject><subject>Oncogene Proteins, Viral - metabolism</subject><subject>Papillomavirus Infections - complications</subject><subject>Papillomavirus Infections - genetics</subject><subject>Papillomavirus Infections - metabolism</subject><subject>Papillomaviruses</subject><subject>PDZ Domains - genetics</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Interaction Domains and Motifs - genetics</subject><subject>Repressor Proteins - chemistry</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - metabolism</subject><subject>Review</subject><subject>Tumors</subject><subject>Uterine Cervical Neoplasms - complications</subject><subject>Uterine Cervical Neoplasms - genetics</subject><subject>Uterine Cervical Neoplasms - virology</subject><issn>2314-6133</issn><issn>2314-6141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqN0s1vFCEYB-CJ0dim9uTdkHgxNmuBl48dDyZNq3aTGvege_BCWOZlSzMLFWZt-t_LuHWzeioXIDz8-MjbNC8ZfceYlKecMjgF1WrGnzSHHJiYKCbY090Y4KA5LuWG1jZlirbqeXPABW2BtuKwWc0vfpCLtLYhFmJjRxYh257Mokc3hBTfkwXmYofQI5mnAeMQbF9I8uRyvpiMm2dxwGz_4EJCJBl7O07IkMgX24dVtNHdv2ie-boRjx_6o-b7p4_fzi8nV18_z87PriZOtmKYsA64E15hp5VgWnIhJQBnQFEiV6iEd8uOar3ECjuuQTrfaetta-lSIBw1H7a5t5vlGjtXL1zfY25zWNt8b5IN5t-VGK7NKv0yoLVmeloD3jwE5PRzg2Uw61Ac9r2NmDbFMKG4VlxqeAQVAJop3lb6-j96kzY51p-oCrRop9DuqZXt0YToU72iG0PNGdQDNVeSVXWyVS6nUjL63esYNWNRmLEozLYoqn61_yE7-7cEKni7BdchdvYuPC4NK0Fv9zAVjHP4DQOVxfc</recordid><startdate>20130101</startdate><enddate>20130101</enddate><creator>Fujii, Tomoyuki</creator><creator>Osuga, Yutaka</creator><creator>Kawana, Kei</creator><creator>Nagasaka, Kazunori</creator><general>Hindawi Publishing Corporation</general><general>John Wiley & Sons, Inc</general><general>Hindawi Limited</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</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>3V.</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TK</scope><scope>7U7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CWDGH</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0696-5175</orcidid></search><sort><creationdate>20130101</creationdate><title>PDZ Domains and Viral Infection: Versatile Potentials of HPV-PDZ Interactions in relation to Malignancy</title><author>Fujii, Tomoyuki ; Osuga, Yutaka ; Kawana, Kei ; Nagasaka, Kazunori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c594t-1d32c4f6ed7641752455332130e5e26e64fcbd077be32cd2735cfd7afa9a0b4e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adaptor Proteins, Signal Transducing - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>BioMed research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fujii, Tomoyuki</au><au>Osuga, Yutaka</au><au>Kawana, Kei</au><au>Nagasaka, Kazunori</au><au>Cantin, Edouard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PDZ Domains and Viral Infection: Versatile Potentials of HPV-PDZ Interactions in relation to Malignancy</atitle><jtitle>BioMed research international</jtitle><addtitle>Biomed Res Int</addtitle><date>2013-01-01</date><risdate>2013</risdate><volume>2013</volume><issue>2013</issue><spage>1</spage><epage>9</epage><pages>1-9</pages><issn>2314-6133</issn><eissn>2314-6141</eissn><abstract>Cervical cancer is caused by high-risk human papillomaviruses (HPVs), and a unique characteristic of these is a PDZ (P̲SD-95/D̲lg/Z̲O-1-)binding motif in their E6 proteins. Through this motif HPV E6 interacts with a variety of PDZ domain-containing proteins and targets them mainly for degradation. These E6-PDZ interactions exhibit extraordinarily different functions in relation to HPV-induced malignancy, depending upon various cellular contexts; for example, Dlg and Scrib show different distribution patterns from what is seen in normal epithelium, both in localization and in amount, and their loss may be a late-stage marker in malignant progression. Recent studies show that interactions with specific forms of the proteins may have oncogenic potential. In addition, it is interesting that PDZ proteins make a contribution to the stabilization of E6 and viral episomal maintenance during the course of HPV life cycle. Various posttranslational modifications also greatly affect their functions. Phosphorylation of hDlg and hScrib by certain kinases regulates several important signaling cascades, and E6-PDZ interactions themselves are regulated through PKA-dependent phosphorylation. Thus these interactions naturally have great potential for both predictive and therapeutic applications, and, with development of screening tools for identifying novel targets of their interactions, comprehensive spatiotemporal analysis is currently underway.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>24093094</pmid><doi>10.1155/2013/369712</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-0696-5175</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | BioMed research international, 2013-01, Vol.2013 (2013), p.1-9 |
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| subjects | Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Causes of Cell cycle Cervical cancer DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Female Health aspects Human papillomavirus Humans Kinases Membrane Proteins - metabolism Oncogene Proteins, Viral - chemistry Oncogene Proteins, Viral - genetics Oncogene Proteins, Viral - metabolism Papillomavirus Infections - complications Papillomavirus Infections - genetics Papillomavirus Infections - metabolism Papillomaviruses PDZ Domains - genetics Phosphorylation Protein Binding Protein Interaction Domains and Motifs - genetics Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism Review Tumors Uterine Cervical Neoplasms - complications Uterine Cervical Neoplasms - genetics Uterine Cervical Neoplasms - virology |
| title | PDZ Domains and Viral Infection: Versatile Potentials of HPV-PDZ Interactions in relation to Malignancy |
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