Mrc1/Claspin: a new role for regulation of origin firing
Mrc1 and its vertebrate homologue Claspin serve as a mediator for replication stress checkpoint signaling, receiving the signal from Mec1/Rad3/ATR sensor kinase and transmitting it to the effector Rad53/Cds1/Chk1 kinase. They are likely to be a part of the replisome and facilitate the S-phase progre...
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| Veröffentlicht in: | Current genetics 2017-10, Vol.63 (5), p.813-818 |
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| creator | Masai, Hisao Yang, Chi-Chun Matsumoto, Seiji |
| description | Mrc1 and its vertebrate homologue Claspin serve as a mediator for replication stress checkpoint signaling, receiving the signal from Mec1/Rad3/ATR sensor kinase and transmitting it to the effector Rad53/Cds1/Chk1 kinase. They are likely to be a part of the replisome and facilitate the S-phase progression by promoting replication fork progression. Recent reports on Mrc1/Claspin indicate their new role in regulating the replication initiation through interaction with Cdc7, a key conserved serine–threonine kinase that triggers firing at each replication origin. Mrc1/Claspin has a specific domain that specifically interacts with Cdc7, and this domain is involved also in intramolecular interaction with its N-terminal segment. Mechanisms for novel regulation of origin firing and its timing through recruitment of Cdc7 to Mrc1/Claspin will be discussed. |
| doi_str_mv | 10.1007/s00294-017-0690-y |
| format | Article |
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They are likely to be a part of the replisome and facilitate the S-phase progression by promoting replication fork progression. Recent reports on Mrc1/Claspin indicate their new role in regulating the replication initiation through interaction with Cdc7, a key conserved serine–threonine kinase that triggers firing at each replication origin. Mrc1/Claspin has a specific domain that specifically interacts with Cdc7, and this domain is involved also in intramolecular interaction with its N-terminal segment. Mechanisms for novel regulation of origin firing and its timing through recruitment of Cdc7 to Mrc1/Claspin will be discussed.</description><identifier>ISSN: 0172-8083</identifier><identifier>EISSN: 1432-0983</identifier><identifier>DOI: 10.1007/s00294-017-0690-y</identifier><identifier>PMID: 28357499</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Adaptor Proteins, Signal Transducing - chemistry ; Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Animals ; Biochemistry ; Biomedical and Life Sciences ; Cell Biology ; Cell Cycle Proteins - metabolism ; CHK1 protein ; DNA Replication ; Firing ; Homology ; Humans ; Life Sciences ; Mammals ; Microbial Genetics and Genomics ; Microbiology ; Mutation ; Phosphotransferases (Alcohol Group Acceptor) - genetics ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; Plant Sciences ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein-Serine-Threonine Kinases - metabolism ; Protein-serine/threonine kinase ; Proteomics ; Receptors, Immunologic - chemistry ; Receptors, Immunologic - genetics ; Receptors, Immunologic - metabolism ; Recruitment ; Replication ; Replication initiation ; Replication Origin ; Replication origins ; Review ; Schizosaccharomyces - genetics ; Schizosaccharomyces - metabolism ; Signal Transduction</subject><ispartof>Current genetics, 2017-10, Vol.63 (5), p.813-818</ispartof><rights>Springer-Verlag Berlin Heidelberg 2017</rights><rights>Current Genetics is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-e874090d2b4e424fd738ef102d27a82879af8a66e275f44a8edb69dceb0c5bc53</citedby><cites>FETCH-LOGICAL-c438t-e874090d2b4e424fd738ef102d27a82879af8a66e275f44a8edb69dceb0c5bc53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00294-017-0690-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00294-017-0690-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28357499$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Masai, Hisao</creatorcontrib><creatorcontrib>Yang, Chi-Chun</creatorcontrib><creatorcontrib>Matsumoto, Seiji</creatorcontrib><title>Mrc1/Claspin: a new role for regulation of origin firing</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><addtitle>Curr Genet</addtitle><description>Mrc1 and its vertebrate homologue Claspin serve as a mediator for replication stress checkpoint signaling, receiving the signal from Mec1/Rad3/ATR sensor kinase and transmitting it to the effector Rad53/Cds1/Chk1 kinase. 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Mechanisms for novel regulation of origin firing and its timing through recruitment of Cdc7 to Mrc1/Claspin will be discussed.</description><subject>Adaptor Proteins, Signal Transducing - chemistry</subject><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>CHK1 protein</subject><subject>DNA Replication</subject><subject>Firing</subject><subject>Homology</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Mammals</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mutation</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - genetics</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>Plant Sciences</subject><subject>Protein Binding</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protein-serine/threonine kinase</subject><subject>Proteomics</subject><subject>Receptors, Immunologic - chemistry</subject><subject>Receptors, Immunologic - genetics</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Recruitment</subject><subject>Replication</subject><subject>Replication initiation</subject><subject>Replication Origin</subject><subject>Replication origins</subject><subject>Review</subject><subject>Schizosaccharomyces - genetics</subject><subject>Schizosaccharomyces - metabolism</subject><subject>Signal Transduction</subject><issn>0172-8083</issn><issn>1432-0983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kE1LxDAQhoMo7rr6A7xIwIuXuJM0bRJvsvgFK170HNI2WbJ0m5pskf33dqmKCJ7mMM_7zvAgdE7hmgKIeQJgihOggkChgOwO0JTyjBFQMjtE02HBiASZTdBJSmsAyqQSx2jCZJYLrtQUyedY0fmiManz7Q02uLUfOIbGYhcijnbVN2brQ4uDwyH6lW-x89G3q1N05EyT7NnXnKG3-7vXxSNZvjw8LW6XpOKZ3BIrBQcFNSu55Yy7WmTSOgqsZsJIJoUyTpqisEzkjnMjbV0Wqq5sCVVeVnk2Q1djbxfDe2_TVm98qmzTmNaGPmkqJeNKcl4M6OUfdB362A7faao48JzSQg0UHakqhpSidbqLfmPiTlPQe6161KoHe3qvVe-GzMVXc19ubP2T-PY4AGwEUreXY-Ov0_-2fgJcnoEm</recordid><startdate>20171001</startdate><enddate>20171001</enddate><creator>Masai, Hisao</creator><creator>Yang, Chi-Chun</creator><creator>Matsumoto, Seiji</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><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>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20171001</creationdate><title>Mrc1/Claspin: a new role for regulation of origin firing</title><author>Masai, Hisao ; Yang, Chi-Chun ; Matsumoto, Seiji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-e874090d2b4e424fd738ef102d27a82879af8a66e275f44a8edb69dceb0c5bc53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Adaptor Proteins, Signal Transducing - chemistry</topic><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Biology</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>CHK1 protein</topic><topic>DNA Replication</topic><topic>Firing</topic><topic>Homology</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Mammals</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mutation</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - genetics</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - metabolism</topic><topic>Plant Sciences</topic><topic>Protein Binding</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protein-serine/threonine kinase</topic><topic>Proteomics</topic><topic>Receptors, Immunologic - chemistry</topic><topic>Receptors, Immunologic - 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Academic</collection><jtitle>Current genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Masai, Hisao</au><au>Yang, Chi-Chun</au><au>Matsumoto, Seiji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mrc1/Claspin: a new role for regulation of origin firing</atitle><jtitle>Current genetics</jtitle><stitle>Curr Genet</stitle><addtitle>Curr Genet</addtitle><date>2017-10-01</date><risdate>2017</risdate><volume>63</volume><issue>5</issue><spage>813</spage><epage>818</epage><pages>813-818</pages><issn>0172-8083</issn><eissn>1432-0983</eissn><abstract>Mrc1 and its vertebrate homologue Claspin serve as a mediator for replication stress checkpoint signaling, receiving the signal from Mec1/Rad3/ATR sensor kinase and transmitting it to the effector Rad53/Cds1/Chk1 kinase. They are likely to be a part of the replisome and facilitate the S-phase progression by promoting replication fork progression. Recent reports on Mrc1/Claspin indicate their new role in regulating the replication initiation through interaction with Cdc7, a key conserved serine–threonine kinase that triggers firing at each replication origin. Mrc1/Claspin has a specific domain that specifically interacts with Cdc7, and this domain is involved also in intramolecular interaction with its N-terminal segment. Mechanisms for novel regulation of origin firing and its timing through recruitment of Cdc7 to Mrc1/Claspin will be discussed.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>28357499</pmid><doi>10.1007/s00294-017-0690-y</doi><tpages>6</tpages></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Animals Biochemistry Biomedical and Life Sciences Cell Biology Cell Cycle Proteins - metabolism CHK1 protein DNA Replication Firing Homology Humans Life Sciences Mammals Microbial Genetics and Genomics Microbiology Mutation Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Plant Sciences Protein Binding Protein Interaction Domains and Motifs Protein-Serine-Threonine Kinases - metabolism Protein-serine/threonine kinase Proteomics Receptors, Immunologic - chemistry Receptors, Immunologic - genetics Receptors, Immunologic - metabolism Recruitment Replication Replication initiation Replication Origin Replication origins Review Schizosaccharomyces - genetics Schizosaccharomyces - metabolism Signal Transduction |
| title | Mrc1/Claspin: a new role for regulation of origin firing |
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