Mixed-lineage kinase 3 phosphorylates prolyl-isomerase Pin1 to regulate its nuclear translocation and cellular function
Nuclear protein peptidyl-prolyl isomerase Pin1-mediated prolyl isomerization is an essential and novel regulatory mechanism for protein phosphorylation. Therefore, tight regulation of Pin1 localization and catalytic activity is crucial for its normal nuclear functions. Pin1 is commonly dysregulated...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-05, Vol.109 (21), p.8149-8154 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Rangasamy, Velusamy Mishra, Rajakishore Sondarva, Gautam Das, Subhasis Lee, Tae Ho Bakowska, Joanna C Tzivion, Guri Malter, James S Rana, Basabi Lu, Kun Ping Kanthasamy, Anumantha Rana, Ajay |
| description | Nuclear protein peptidyl-prolyl isomerase Pin1-mediated prolyl isomerization is an essential and novel regulatory mechanism for protein phosphorylation. Therefore, tight regulation of Pin1 localization and catalytic activity is crucial for its normal nuclear functions. Pin1 is commonly dysregulated during oncogenesis and likely contributes to these pathologies; however, the mechanism(s) by which Pin1 catalytic activity and nuclear localization are increased is unknown. Here we demonstrate that mixed-lineage kinase 3 (MLK3), a MAP3K family member, phosphorylates Pin1 on a Ser138 site to increase its catalytic activity and nuclear translocation. This phosphorylation event drives the cell cycle and promotes cyclin D1 stability and centrosome amplification. Notably, Pin1 pSer138 is significantly up-regulated in breast tumors and is localized in the nucleus. These findings collectively suggest that the MLK3-Pin1 signaling cascade plays a critical role in regulating the cell cycle, centrosome numbers, and oncogenesis. |
| doi_str_mv | 10.1073/pnas.1200804109 |
| format | Article |
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Therefore, tight regulation of Pin1 localization and catalytic activity is crucial for its normal nuclear functions. Pin1 is commonly dysregulated during oncogenesis and likely contributes to these pathologies; however, the mechanism(s) by which Pin1 catalytic activity and nuclear localization are increased is unknown. Here we demonstrate that mixed-lineage kinase 3 (MLK3), a MAP3K family member, phosphorylates Pin1 on a Ser138 site to increase its catalytic activity and nuclear translocation. This phosphorylation event drives the cell cycle and promotes cyclin D1 stability and centrosome amplification. Notably, Pin1 pSer138 is significantly up-regulated in breast tumors and is localized in the nucleus. These findings collectively suggest that the MLK3-Pin1 signaling cascade plays a critical role in regulating the cell cycle, centrosome numbers, and oncogenesis.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1200804109</identifier><identifier>PMID: 22566623</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Active Transport, Cell Nucleus ; Active Transport, Cell Nucleus - physiology ; Antibodies ; Biological Sciences ; breast neoplasms ; Breast Neoplasms - genetics ; Breast Neoplasms - metabolism ; Catalysis ; Catalytic activity ; Cell cycle ; Cell Cycle - physiology ; Cell cycle proteins ; Cell lines ; Cell Nucleus ; Cell Nucleus - metabolism ; Cell Transformation, Neoplastic ; Cell Transformation, Neoplastic - genetics ; Cell Transformation, Neoplastic - metabolism ; Centrosome ; Centrosome - metabolism ; Centrosomes ; Cyclin D1 ; Cyclin D1 - metabolism ; Cyclins ; Female ; genetics ; Green Fluorescent Proteins ; Green Fluorescent Proteins - genetics ; HEK293 Cells ; HeLa Cells ; Humans ; isomerization ; Kinases ; MAP Kinase Kinase Kinases ; MAP Kinase Kinase Kinases - genetics ; MAP Kinase Kinase Kinases - metabolism ; metabolism ; mitogen-activated protein kinase kinase kinase ; Mitogen-Activated Protein Kinase Kinase Kinase 11 ; NIMA-Interacting Peptidylprolyl Isomerase ; Peptidylprolyl Isomerase ; Peptidylprolyl Isomerase - genetics ; Peptidylprolyl Isomerase - metabolism ; Phosphorylation ; Phosphorylation - physiology ; physiology ; protein phosphorylation ; Proteins ; Serine ; Serine - metabolism ; Signal Transduction ; Signal Transduction - physiology ; Tumors</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-05, Vol.109 (21), p.8149-8154</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences May 22, 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c590t-ac370811166593e13630a6a99bd9c82d7f68b1e73fbe3c6bf831e2306858a2e43</citedby><cites>FETCH-LOGICAL-c590t-ac370811166593e13630a6a99bd9c82d7f68b1e73fbe3c6bf831e2306858a2e43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/21.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41602956$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41602956$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22566623$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rangasamy, Velusamy</creatorcontrib><creatorcontrib>Mishra, Rajakishore</creatorcontrib><creatorcontrib>Sondarva, Gautam</creatorcontrib><creatorcontrib>Das, Subhasis</creatorcontrib><creatorcontrib>Lee, Tae Ho</creatorcontrib><creatorcontrib>Bakowska, Joanna C</creatorcontrib><creatorcontrib>Tzivion, Guri</creatorcontrib><creatorcontrib>Malter, James S</creatorcontrib><creatorcontrib>Rana, Basabi</creatorcontrib><creatorcontrib>Lu, Kun Ping</creatorcontrib><creatorcontrib>Kanthasamy, Anumantha</creatorcontrib><creatorcontrib>Rana, Ajay</creatorcontrib><title>Mixed-lineage kinase 3 phosphorylates prolyl-isomerase Pin1 to regulate its nuclear translocation and cellular function</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Nuclear protein peptidyl-prolyl isomerase Pin1-mediated prolyl isomerization is an essential and novel regulatory mechanism for protein phosphorylation. Therefore, tight regulation of Pin1 localization and catalytic activity is crucial for its normal nuclear functions. Pin1 is commonly dysregulated during oncogenesis and likely contributes to these pathologies; however, the mechanism(s) by which Pin1 catalytic activity and nuclear localization are increased is unknown. Here we demonstrate that mixed-lineage kinase 3 (MLK3), a MAP3K family member, phosphorylates Pin1 on a Ser138 site to increase its catalytic activity and nuclear translocation. This phosphorylation event drives the cell cycle and promotes cyclin D1 stability and centrosome amplification. Notably, Pin1 pSer138 is significantly up-regulated in breast tumors and is localized in the nucleus. These findings collectively suggest that the MLK3-Pin1 signaling cascade plays a critical role in regulating the cell cycle, centrosome numbers, and oncogenesis.</description><subject>Active Transport, Cell Nucleus</subject><subject>Active Transport, Cell Nucleus - physiology</subject><subject>Antibodies</subject><subject>Biological Sciences</subject><subject>breast neoplasms</subject><subject>Breast Neoplasms - genetics</subject><subject>Breast Neoplasms - metabolism</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Cell cycle</subject><subject>Cell Cycle - physiology</subject><subject>Cell cycle proteins</subject><subject>Cell lines</subject><subject>Cell Nucleus</subject><subject>Cell Nucleus - metabolism</subject><subject>Cell Transformation, Neoplastic</subject><subject>Cell Transformation, Neoplastic - genetics</subject><subject>Cell Transformation, Neoplastic - metabolism</subject><subject>Centrosome</subject><subject>Centrosome - metabolism</subject><subject>Centrosomes</subject><subject>Cyclin D1</subject><subject>Cyclin D1 - metabolism</subject><subject>Cyclins</subject><subject>Female</subject><subject>genetics</subject><subject>Green Fluorescent Proteins</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>isomerization</subject><subject>Kinases</subject><subject>MAP Kinase Kinase Kinases</subject><subject>MAP Kinase Kinase Kinases - genetics</subject><subject>MAP Kinase Kinase Kinases - metabolism</subject><subject>metabolism</subject><subject>mitogen-activated protein kinase kinase kinase</subject><subject>Mitogen-Activated Protein Kinase Kinase Kinase 11</subject><subject>NIMA-Interacting Peptidylprolyl Isomerase</subject><subject>Peptidylprolyl Isomerase</subject><subject>Peptidylprolyl Isomerase - genetics</subject><subject>Peptidylprolyl Isomerase - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphorylation - physiology</subject><subject>physiology</subject><subject>protein phosphorylation</subject><subject>Proteins</subject><subject>Serine</subject><subject>Serine - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rangasamy, Velusamy</au><au>Mishra, Rajakishore</au><au>Sondarva, Gautam</au><au>Das, Subhasis</au><au>Lee, Tae Ho</au><au>Bakowska, Joanna C</au><au>Tzivion, Guri</au><au>Malter, James S</au><au>Rana, Basabi</au><au>Lu, Kun Ping</au><au>Kanthasamy, Anumantha</au><au>Rana, Ajay</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mixed-lineage kinase 3 phosphorylates prolyl-isomerase Pin1 to regulate its nuclear translocation and cellular function</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-05-22</date><risdate>2012</risdate><volume>109</volume><issue>21</issue><spage>8149</spage><epage>8154</epage><pages>8149-8154</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Nuclear protein peptidyl-prolyl isomerase Pin1-mediated prolyl isomerization is an essential and novel regulatory mechanism for protein phosphorylation. Therefore, tight regulation of Pin1 localization and catalytic activity is crucial for its normal nuclear functions. Pin1 is commonly dysregulated during oncogenesis and likely contributes to these pathologies; however, the mechanism(s) by which Pin1 catalytic activity and nuclear localization are increased is unknown. Here we demonstrate that mixed-lineage kinase 3 (MLK3), a MAP3K family member, phosphorylates Pin1 on a Ser138 site to increase its catalytic activity and nuclear translocation. This phosphorylation event drives the cell cycle and promotes cyclin D1 stability and centrosome amplification. Notably, Pin1 pSer138 is significantly up-regulated in breast tumors and is localized in the nucleus. These findings collectively suggest that the MLK3-Pin1 signaling cascade plays a critical role in regulating the cell cycle, centrosome numbers, and oncogenesis.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22566623</pmid><doi>10.1073/pnas.1200804109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Active Transport, Cell Nucleus Active Transport, Cell Nucleus - physiology Antibodies Biological Sciences breast neoplasms Breast Neoplasms - genetics Breast Neoplasms - metabolism Catalysis Catalytic activity Cell cycle Cell Cycle - physiology Cell cycle proteins Cell lines Cell Nucleus Cell Nucleus - metabolism Cell Transformation, Neoplastic Cell Transformation, Neoplastic - genetics Cell Transformation, Neoplastic - metabolism Centrosome Centrosome - metabolism Centrosomes Cyclin D1 Cyclin D1 - metabolism Cyclins Female genetics Green Fluorescent Proteins Green Fluorescent Proteins - genetics HEK293 Cells HeLa Cells Humans isomerization Kinases MAP Kinase Kinase Kinases MAP Kinase Kinase Kinases - genetics MAP Kinase Kinase Kinases - metabolism metabolism mitogen-activated protein kinase kinase kinase Mitogen-Activated Protein Kinase Kinase Kinase 11 NIMA-Interacting Peptidylprolyl Isomerase Peptidylprolyl Isomerase Peptidylprolyl Isomerase - genetics Peptidylprolyl Isomerase - metabolism Phosphorylation Phosphorylation - physiology physiology protein phosphorylation Proteins Serine Serine - metabolism Signal Transduction Signal Transduction - physiology Tumors |
| title | Mixed-lineage kinase 3 phosphorylates prolyl-isomerase Pin1 to regulate its nuclear translocation and cellular function |
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