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TOPK and PTEN participate in CHFR mediated mitotic checkpoint
Mitotic progression is regulated by co-ordinated action of several proteins and is crucial for the maintenance of genomic stability. CHFR (Check point protein with FHA and RING domains) is an E3 ubiquitin ligase and a checkpoint protein that regulates entry into mitosis. But the molecular players in...
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Published in: | Cellular signalling 2013-12, Vol.25 (12), p.2511-2517 |
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creator | Shinde, Swapnil R. Gangula, Narmadha Reddy Kavela, Sridhar Pandey, Vimal Maddika, Subbareddy |
description | Mitotic progression is regulated by co-ordinated action of several proteins and is crucial for the maintenance of genomic stability. CHFR (Check point protein with FHA and RING domains) is an E3 ubiquitin ligase and a checkpoint protein that regulates entry into mitosis. But the molecular players involved in CHFR mediated mitotic checkpoint are not completely understood. In this study, we identified TOPK/PBK, a serine/threonine kinase and PTEN, a lipid phosphatase to play an important role in CHFR mediated mitotic transitions. We demonstrated that CHFR ubiquitinates and regulates TOPK levels, which is essential for its checkpoint function. Moreover, TOPK phosphorylates and inactivates PTEN, which in turn activates Akt that leads to proper G2/M progression. Collectively, our results reveal TOPK and PTEN as new players in CHFR mediated mitotic checkpoint.
•TOPK is identified as a novel CHFR associated protein.•TOPK is a substrate of CHFR.•TOPK participates in CHFR mediated mitotic stress check point.•PTEN is phosphorylated by TOPK and is required for mitotic entry. |
doi_str_mv | 10.1016/j.cellsig.2013.08.013 |
format | article |
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•TOPK is identified as a novel CHFR associated protein.•TOPK is a substrate of CHFR.•TOPK participates in CHFR mediated mitotic stress check point.•PTEN is phosphorylated by TOPK and is required for mitotic entry.</description><identifier>ISSN: 0898-6568</identifier><identifier>EISSN: 1873-3913</identifier><identifier>DOI: 10.1016/j.cellsig.2013.08.013</identifier><identifier>PMID: 24012691</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Akt ; Cell Cycle Proteins - metabolism ; Chfr ; E3 ligase ; HeLa Cells ; Humans ; Kinases ; Lipids ; M Phase Cell Cycle Checkpoints ; Maintenance ; Mitogen-Activated Protein Kinase Kinases - metabolism ; Mitosis ; Neoplasm Proteins - metabolism ; Phosphorylation ; Players ; Poly-ADP-Ribose Binding Proteins ; Progressions ; Proteins ; Proto-Oncogene Proteins c-akt - metabolism ; PTEN ; PTEN Phosphohydrolase - metabolism ; Stability ; TOPK ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases ; Ubiquitination</subject><ispartof>Cellular signalling, 2013-12, Vol.25 (12), p.2511-2517</ispartof><rights>2013 The Authors</rights><rights>2013. Published by Elsevier Inc. All rights reserved.</rights><rights>2013 The Authors 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c566t-3b53ef48868f810b50ddb96d2aab2ffafc130155efd9d98c7318dbab844bcf873</citedby><cites>FETCH-LOGICAL-c566t-3b53ef48868f810b50ddb96d2aab2ffafc130155efd9d98c7318dbab844bcf873</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24012691$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shinde, Swapnil R.</creatorcontrib><creatorcontrib>Gangula, Narmadha Reddy</creatorcontrib><creatorcontrib>Kavela, Sridhar</creatorcontrib><creatorcontrib>Pandey, Vimal</creatorcontrib><creatorcontrib>Maddika, Subbareddy</creatorcontrib><title>TOPK and PTEN participate in CHFR mediated mitotic checkpoint</title><title>Cellular signalling</title><addtitle>Cell Signal</addtitle><description>Mitotic progression is regulated by co-ordinated action of several proteins and is crucial for the maintenance of genomic stability. CHFR (Check point protein with FHA and RING domains) is an E3 ubiquitin ligase and a checkpoint protein that regulates entry into mitosis. But the molecular players involved in CHFR mediated mitotic checkpoint are not completely understood. In this study, we identified TOPK/PBK, a serine/threonine kinase and PTEN, a lipid phosphatase to play an important role in CHFR mediated mitotic transitions. We demonstrated that CHFR ubiquitinates and regulates TOPK levels, which is essential for its checkpoint function. Moreover, TOPK phosphorylates and inactivates PTEN, which in turn activates Akt that leads to proper G2/M progression. Collectively, our results reveal TOPK and PTEN as new players in CHFR mediated mitotic checkpoint.
•TOPK is identified as a novel CHFR associated protein.•TOPK is a substrate of CHFR.•TOPK participates in CHFR mediated mitotic stress check point.•PTEN is phosphorylated by TOPK and is required for mitotic entry.</description><subject>Akt</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Chfr</subject><subject>E3 ligase</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Kinases</subject><subject>Lipids</subject><subject>M Phase Cell Cycle Checkpoints</subject><subject>Maintenance</subject><subject>Mitogen-Activated Protein Kinase Kinases - metabolism</subject><subject>Mitosis</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Phosphorylation</subject><subject>Players</subject><subject>Poly-ADP-Ribose Binding Proteins</subject><subject>Progressions</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>PTEN</subject><subject>PTEN Phosphohydrolase - metabolism</subject><subject>Stability</subject><subject>TOPK</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitin-Protein Ligases</subject><subject>Ubiquitination</subject><issn>0898-6568</issn><issn>1873-3913</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNqFUctOwzAQtBCIlscngHLkkmDHjmMfAKGKl6hohcrZcvygLm0S7BSJv8elBcGpp9FqZ2dndwA4QTBDENHzWabMfB7ca5ZDhDPIsgg7oI9YiVPMEd4Ffcg4S2lBWQ8chDCDEBWQ5vuglxOIcspRH1xMRuPHRNY6GU9unpJW-s4p18rOJK5OBve3z8nCaBdrnSxc18RuoqZGvbWNq7sjsGflPJjjDR6Cl9ubyeA-HY7uHgbXw1QVlHYprgpsLGGMMssQrAqodcWpzqWscmulVQhHb4WxmmvOVIkR05WsGCGVsvGgQ3C51m2XVbSjTN15ORetdwvpP0Ujnfjfqd1UvDYfAjPE-bfA2UbAN-9LEzqxcGH1QFmbZhkEoiUiJSN5vp1KCOa8JBxHarGmKt-E4I39dYSgWKUkZmKTklilJCATEeLc6d9zfqd-YomEqzXBxKd-OONFUM7UKibhjeqEbtyWFV9CUaYK</recordid><startdate>20131201</startdate><enddate>20131201</enddate><creator>Shinde, Swapnil R.</creator><creator>Gangula, Narmadha Reddy</creator><creator>Kavela, Sridhar</creator><creator>Pandey, Vimal</creator><creator>Maddika, Subbareddy</creator><general>Elsevier Inc</general><general>Elsevier Science Ltd</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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>5PM</scope></search><sort><creationdate>20131201</creationdate><title>TOPK and PTEN participate in CHFR mediated mitotic checkpoint</title><author>Shinde, Swapnil R. ; Gangula, Narmadha Reddy ; Kavela, Sridhar ; Pandey, Vimal ; Maddika, Subbareddy</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c566t-3b53ef48868f810b50ddb96d2aab2ffafc130155efd9d98c7318dbab844bcf873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Akt</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Chfr</topic><topic>E3 ligase</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Kinases</topic><topic>Lipids</topic><topic>M Phase Cell Cycle Checkpoints</topic><topic>Maintenance</topic><topic>Mitogen-Activated Protein Kinase Kinases - metabolism</topic><topic>Mitosis</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Phosphorylation</topic><topic>Players</topic><topic>Poly-ADP-Ribose Binding Proteins</topic><topic>Progressions</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>PTEN</topic><topic>PTEN Phosphohydrolase - metabolism</topic><topic>Stability</topic><topic>TOPK</topic><topic>Ubiquitin - metabolism</topic><topic>Ubiquitin-Protein Ligases</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shinde, Swapnil R.</creatorcontrib><creatorcontrib>Gangula, Narmadha Reddy</creatorcontrib><creatorcontrib>Kavela, Sridhar</creatorcontrib><creatorcontrib>Pandey, Vimal</creatorcontrib><creatorcontrib>Maddika, Subbareddy</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>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cellular signalling</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shinde, Swapnil R.</au><au>Gangula, Narmadha Reddy</au><au>Kavela, Sridhar</au><au>Pandey, Vimal</au><au>Maddika, Subbareddy</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TOPK and PTEN participate in CHFR mediated mitotic checkpoint</atitle><jtitle>Cellular signalling</jtitle><addtitle>Cell Signal</addtitle><date>2013-12-01</date><risdate>2013</risdate><volume>25</volume><issue>12</issue><spage>2511</spage><epage>2517</epage><pages>2511-2517</pages><issn>0898-6568</issn><eissn>1873-3913</eissn><abstract>Mitotic progression is regulated by co-ordinated action of several proteins and is crucial for the maintenance of genomic stability. CHFR (Check point protein with FHA and RING domains) is an E3 ubiquitin ligase and a checkpoint protein that regulates entry into mitosis. But the molecular players involved in CHFR mediated mitotic checkpoint are not completely understood. In this study, we identified TOPK/PBK, a serine/threonine kinase and PTEN, a lipid phosphatase to play an important role in CHFR mediated mitotic transitions. We demonstrated that CHFR ubiquitinates and regulates TOPK levels, which is essential for its checkpoint function. Moreover, TOPK phosphorylates and inactivates PTEN, which in turn activates Akt that leads to proper G2/M progression. Collectively, our results reveal TOPK and PTEN as new players in CHFR mediated mitotic checkpoint.
•TOPK is identified as a novel CHFR associated protein.•TOPK is a substrate of CHFR.•TOPK participates in CHFR mediated mitotic stress check point.•PTEN is phosphorylated by TOPK and is required for mitotic entry.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>24012691</pmid><doi>10.1016/j.cellsig.2013.08.013</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Akt Cell Cycle Proteins - metabolism Chfr E3 ligase HeLa Cells Humans Kinases Lipids M Phase Cell Cycle Checkpoints Maintenance Mitogen-Activated Protein Kinase Kinases - metabolism Mitosis Neoplasm Proteins - metabolism Phosphorylation Players Poly-ADP-Ribose Binding Proteins Progressions Proteins Proto-Oncogene Proteins c-akt - metabolism PTEN PTEN Phosphohydrolase - metabolism Stability TOPK Ubiquitin - metabolism Ubiquitin-Protein Ligases Ubiquitination |
title | TOPK and PTEN participate in CHFR mediated mitotic checkpoint |
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