Patched1 interacts with cyclin B1 to regulate cell cycle progression
The initiation of mitosis requires the activation of M‐phase promoting factor (MPF). MPF activation and its subcellular localization are dependent on the phosphorylation state of its components, cdc2 and cyclin B1. In a two‐hybrid screen using a bait protein to mimic phosphorylated cyclin B1, we ide...
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| Veröffentlicht in: | The EMBO journal 2001-05, Vol.20 (9), p.2214-2223 |
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| description | The initiation of mitosis requires the activation of M‐phase promoting factor (MPF). MPF activation and its subcellular localization are dependent on the phosphorylation state of its components, cdc2 and cyclin B1. In a two‐hybrid screen using a bait protein to mimic phosphorylated cyclin B1, we identified a novel interaction between cyclin B1 and patched1 (ptc1), a tumor suppressor associated with basal cell carcinoma (BCC). Ptc1 interacted specifically with constitutively phosphorylated cyclin B1 derivatives and was able to alter their normal subcellular localization. Furthermore, addition of the ptc1 ligand, sonic hedgehog (shh), disrupts this interaction and allows cyclin B1 to localize to the nucleus. Expression of ptc1 in 293T cells was inhibitory to cell proliferation; this inhibition could be relieved by coexpression of a cyclin B1 derivative that constitutively localizes to the nucleus and that could not interact with ptc1 due to phosphorylation‐site mutations to Ala. In addition, we demonstrate that endogenous ptc1 and endogenous cyclin B1 interact
in vivo
. The findings reported here demonstrate that ptc1 participates in determining the subcellular localization of cyclin B1 and suggest a link between the tumor suppressor activity of ptc1 and the regulation of cell division. Thus, we propose that ptc1 participates in a G
2
/M checkpoint by regulating the localization of MPF. |
| doi_str_mv | 10.1093/emboj/20.9.2214 |
| format | Article |
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in vivo
. The findings reported here demonstrate that ptc1 participates in determining the subcellular localization of cyclin B1 and suggest a link between the tumor suppressor activity of ptc1 and the regulation of cell division. Thus, we propose that ptc1 participates in a G
2
/M checkpoint by regulating the localization of MPF.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/20.9.2214</identifier><identifier>PMID: 11331587</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Animals ; Baits ; basal cell carcinoma ; cdc2 gene ; Cell Cycle - drug effects ; Cell Cycle - physiology ; Cell Division - drug effects ; Cell Division - physiology ; Cell Line ; Cyclin B - metabolism ; Cyclin B1 ; cytoplasmic retention signal ; Hedgehog Proteins ; Humans ; Kidney - cytology ; Kidney - metabolism ; Life Sciences ; M checkpoint ; M-phase promoting factor ; Macromolecular Substances ; Maturation-Promoting Factor - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membrane Proteins - pharmacology ; Mice ; nevoid basal cell carcinoma syndrome ; Patched Receptors ; Patched-1 Receptor ; patched1 gene ; Phosphorylation ; Precipitin Tests ; Protein Binding - drug effects ; Protein Binding - physiology ; Protein Structure, Tertiary - physiology ; Proteins - metabolism ; Proteins - pharmacology ; ptc1 gene ; Receptors, Cell Surface ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Trans-Activators ; Transfection ; Two-Hybrid System Techniques ; Xenopus</subject><ispartof>The EMBO journal, 2001-05, Vol.20 (9), p.2214-2223</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) May 01, 2001</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6301-71ff8d1f237b30cc80f6f911405f48bbd5c4eb7af50607377ee592e4f390e9ca3</citedby><orcidid>0000-0001-9751-2202</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/PMC125436/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125436/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11331587$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02678324$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Barnes, Elizabeth A.</creatorcontrib><creatorcontrib>Kong, Monica</creatorcontrib><creatorcontrib>Ollendorff, Vincent</creatorcontrib><creatorcontrib>Donoghue, Daniel J</creatorcontrib><title>Patched1 interacts with cyclin B1 to regulate cell cycle progression</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>The initiation of mitosis requires the activation of M‐phase promoting factor (MPF). MPF activation and its subcellular localization are dependent on the phosphorylation state of its components, cdc2 and cyclin B1. In a two‐hybrid screen using a bait protein to mimic phosphorylated cyclin B1, we identified a novel interaction between cyclin B1 and patched1 (ptc1), a tumor suppressor associated with basal cell carcinoma (BCC). Ptc1 interacted specifically with constitutively phosphorylated cyclin B1 derivatives and was able to alter their normal subcellular localization. Furthermore, addition of the ptc1 ligand, sonic hedgehog (shh), disrupts this interaction and allows cyclin B1 to localize to the nucleus. Expression of ptc1 in 293T cells was inhibitory to cell proliferation; this inhibition could be relieved by coexpression of a cyclin B1 derivative that constitutively localizes to the nucleus and that could not interact with ptc1 due to phosphorylation‐site mutations to Ala. In addition, we demonstrate that endogenous ptc1 and endogenous cyclin B1 interact
in vivo
. The findings reported here demonstrate that ptc1 participates in determining the subcellular localization of cyclin B1 and suggest a link between the tumor suppressor activity of ptc1 and the regulation of cell division. Thus, we propose that ptc1 participates in a G
2
/M checkpoint by regulating the localization of MPF.</description><subject>Animals</subject><subject>Baits</subject><subject>basal cell carcinoma</subject><subject>cdc2 gene</subject><subject>Cell Cycle - drug effects</subject><subject>Cell Cycle - physiology</subject><subject>Cell Division - drug effects</subject><subject>Cell Division - physiology</subject><subject>Cell Line</subject><subject>Cyclin B - metabolism</subject><subject>Cyclin B1</subject><subject>cytoplasmic retention signal</subject><subject>Hedgehog Proteins</subject><subject>Humans</subject><subject>Kidney - cytology</subject><subject>Kidney - metabolism</subject><subject>Life Sciences</subject><subject>M checkpoint</subject><subject>M-phase promoting factor</subject><subject>Macromolecular Substances</subject><subject>Maturation-Promoting Factor - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Proteins - pharmacology</subject><subject>Mice</subject><subject>nevoid basal cell carcinoma syndrome</subject><subject>Patched Receptors</subject><subject>Patched-1 Receptor</subject><subject>patched1 gene</subject><subject>Phosphorylation</subject><subject>Precipitin Tests</subject><subject>Protein Binding - drug effects</subject><subject>Protein Binding - physiology</subject><subject>Protein Structure, Tertiary - physiology</subject><subject>Proteins - metabolism</subject><subject>Proteins - pharmacology</subject><subject>ptc1 gene</subject><subject>Receptors, Cell Surface</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Trans-Activators</subject><subject>Transfection</subject><subject>Two-Hybrid System Techniques</subject><subject>Xenopus</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkc9v0zAUxyMEYmVw5gSKOCDtkPY9O47jA4f9ogNK2WEIiYvluC9tSpoUO9nof0-6VN2YhHay5e_n-97z-wbBa4QhguIjWmX1csRgqIaMYfwkGGCcQMRAiqfBAFiCUYypOgheeL8EAJFKfB4cIHKO3X0QnF2axi5ohmFRNeSMbXx4UzSL0G5sWVThCYZNHTqat6VpKLRUlrcShWtXzx15X9TVy-BZbkpPr3bnYfD94_nV6UU0-Tb-dHo8iWzCASOJeZ7OMGdcZhysTSFPcoUYg8jjNMtmwsaUSZMLSEByKYmEYhTnXAEpa_hh8KGvu26zFc0sVY0zpV67YmXcRtem0P8qVbHQ8_paIxMxTzr_Ue9fPHBdHE_09q1bmEw5i6-xY9_vern6d0u-0avCb79vKqpbryWkyJWCR0GUaaJiwTrw3QNwWbeu6hamUQkmIJWig0Y9ZF3tvaN8PyeC3kaubyPXDLTS28g7x9v7S7njdxl3QNoDN0VJm8fq6fOvJ5-lUFyy7RKgt_rOVc3J3Rv5v-O86S2VaVpH-3Z3JaNeL3xDf_aycb900mUu9I_pWOPlmH-5mv7UU_4XG0jhkw</recordid><startdate>20010501</startdate><enddate>20010501</enddate><creator>Barnes, Elizabeth A.</creator><creator>Kong, Monica</creator><creator>Ollendorff, Vincent</creator><creator>Donoghue, Daniel J</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>EMBO Press</general><general>Oxford University Press</general><scope>BSCLL</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-9751-2202</orcidid></search><sort><creationdate>20010501</creationdate><title>Patched1 interacts with cyclin B1 to regulate cell cycle progression</title><author>Barnes, Elizabeth A. ; Kong, Monica ; Ollendorff, Vincent ; Donoghue, Daniel J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6301-71ff8d1f237b30cc80f6f911405f48bbd5c4eb7af50607377ee592e4f390e9ca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Baits</topic><topic>basal cell carcinoma</topic><topic>cdc2 gene</topic><topic>Cell Cycle - drug effects</topic><topic>Cell Cycle - physiology</topic><topic>Cell Division - drug effects</topic><topic>Cell Division - physiology</topic><topic>Cell Line</topic><topic>Cyclin B - metabolism</topic><topic>Cyclin B1</topic><topic>cytoplasmic retention signal</topic><topic>Hedgehog Proteins</topic><topic>Humans</topic><topic>Kidney - cytology</topic><topic>Kidney - metabolism</topic><topic>Life Sciences</topic><topic>M checkpoint</topic><topic>M-phase promoting factor</topic><topic>Macromolecular Substances</topic><topic>Maturation-Promoting Factor - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Proteins - pharmacology</topic><topic>Mice</topic><topic>nevoid basal cell carcinoma syndrome</topic><topic>Patched Receptors</topic><topic>Patched-1 Receptor</topic><topic>patched1 gene</topic><topic>Phosphorylation</topic><topic>Precipitin Tests</topic><topic>Protein Binding - drug effects</topic><topic>Protein Binding - physiology</topic><topic>Protein Structure, Tertiary - physiology</topic><topic>Proteins - metabolism</topic><topic>Proteins - pharmacology</topic><topic>ptc1 gene</topic><topic>Receptors, Cell Surface</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Trans-Activators</topic><topic>Transfection</topic><topic>Two-Hybrid System Techniques</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barnes, Elizabeth A.</creatorcontrib><creatorcontrib>Kong, Monica</creatorcontrib><creatorcontrib>Ollendorff, Vincent</creatorcontrib><creatorcontrib>Donoghue, Daniel J</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barnes, Elizabeth A.</au><au>Kong, Monica</au><au>Ollendorff, Vincent</au><au>Donoghue, Daniel J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Patched1 interacts with cyclin B1 to regulate cell cycle progression</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2001-05-01</date><risdate>2001</risdate><volume>20</volume><issue>9</issue><spage>2214</spage><epage>2223</epage><pages>2214-2223</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The initiation of mitosis requires the activation of M‐phase promoting factor (MPF). MPF activation and its subcellular localization are dependent on the phosphorylation state of its components, cdc2 and cyclin B1. In a two‐hybrid screen using a bait protein to mimic phosphorylated cyclin B1, we identified a novel interaction between cyclin B1 and patched1 (ptc1), a tumor suppressor associated with basal cell carcinoma (BCC). Ptc1 interacted specifically with constitutively phosphorylated cyclin B1 derivatives and was able to alter their normal subcellular localization. Furthermore, addition of the ptc1 ligand, sonic hedgehog (shh), disrupts this interaction and allows cyclin B1 to localize to the nucleus. Expression of ptc1 in 293T cells was inhibitory to cell proliferation; this inhibition could be relieved by coexpression of a cyclin B1 derivative that constitutively localizes to the nucleus and that could not interact with ptc1 due to phosphorylation‐site mutations to Ala. In addition, we demonstrate that endogenous ptc1 and endogenous cyclin B1 interact
in vivo
. The findings reported here demonstrate that ptc1 participates in determining the subcellular localization of cyclin B1 and suggest a link between the tumor suppressor activity of ptc1 and the regulation of cell division. Thus, we propose that ptc1 participates in a G
2
/M checkpoint by regulating the localization of MPF.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11331587</pmid><doi>10.1093/emboj/20.9.2214</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-9751-2202</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Baits basal cell carcinoma cdc2 gene Cell Cycle - drug effects Cell Cycle - physiology Cell Division - drug effects Cell Division - physiology Cell Line Cyclin B - metabolism Cyclin B1 cytoplasmic retention signal Hedgehog Proteins Humans Kidney - cytology Kidney - metabolism Life Sciences M checkpoint M-phase promoting factor Macromolecular Substances Maturation-Promoting Factor - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Membrane Proteins - pharmacology Mice nevoid basal cell carcinoma syndrome Patched Receptors Patched-1 Receptor patched1 gene Phosphorylation Precipitin Tests Protein Binding - drug effects Protein Binding - physiology Protein Structure, Tertiary - physiology Proteins - metabolism Proteins - pharmacology ptc1 gene Receptors, Cell Surface Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Trans-Activators Transfection Two-Hybrid System Techniques Xenopus |
| title | Patched1 interacts with cyclin B1 to regulate cell cycle progression |
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