WRM-1 Activates the LIT-1 Protein Kinase to Transduce Anterior/Posterior Polarity Signals in C. elegans
During C. elegans development, Wnt/WG signaling is required for differences in cell fate between sister cells born from anterior/posterior divisions. A β-catenin-related gene, wrm-1, and the lit-1 gene are effectors of this signaling pathway and appear to downregulate the activity of POP-1, a TCF/LE...
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| Veröffentlicht in: | Cell 1999-06, Vol.97 (6), p.717-726 |
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| container_title | Cell |
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| creator | Rocheleau, Christian E Yasuda, Jun Shin, Tae Ho Lin, Rueyling Sawa, Hitoshi Okano, Hideyuki Priess, James R Davis, Roger J Mello, Craig C |
| description | During
C. elegans development, Wnt/WG signaling is required for differences in cell fate between sister cells born from anterior/posterior divisions. A β-catenin-related gene,
wrm-1, and the
lit-1 gene are effectors of this signaling pathway and appear to downregulate the activity of POP-1, a TCF/LEF–related protein, in posterior daughter cells. We show here that
lit-1 encodes a serine/threonine protein kinase homolog related to the
Drosophila tissue polarity protein Nemo. We demonstrate that the WRM-1 protein binds to LIT-1 in vivo and that WRM-1 can activate the LIT-1 protein kinase when coexpressed in vertebrate tissue culture cells. This activation leads to phosphorylation of POP-1 and to apparent changes in its subcellular localization. Our findings provide evidence for novel regulatory avenues for an evolutionarily conserved Wnt/WG signaling pathway. |
| doi_str_mv | 10.1016/S0092-8674(00)80784-9 |
| format | Article |
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C. elegans development, Wnt/WG signaling is required for differences in cell fate between sister cells born from anterior/posterior divisions. A β-catenin-related gene,
wrm-1, and the
lit-1 gene are effectors of this signaling pathway and appear to downregulate the activity of POP-1, a TCF/LEF–related protein, in posterior daughter cells. We show here that
lit-1 encodes a serine/threonine protein kinase homolog related to the
Drosophila tissue polarity protein Nemo. We demonstrate that the WRM-1 protein binds to LIT-1 in vivo and that WRM-1 can activate the LIT-1 protein kinase when coexpressed in vertebrate tissue culture cells. This activation leads to phosphorylation of POP-1 and to apparent changes in its subcellular localization. Our findings provide evidence for novel regulatory avenues for an evolutionarily conserved Wnt/WG signaling pathway.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(00)80784-9</identifier><identifier>PMID: 10380924</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; beta Catenin ; Caenorhabditis elegans ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins ; COS Cells ; Cytoskeletal Proteins - genetics ; Cytoskeletal Proteins - metabolism ; DNA-Binding Proteins - metabolism ; Drosophila ; Enzyme Activation ; Helminth Proteins - genetics ; Helminth Proteins - metabolism ; High Mobility Group Proteins - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Signal Transduction ; Trans-Activators</subject><ispartof>Cell, 1999-06, Vol.97 (6), p.717-726</ispartof><rights>1999 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-2a4e1c50d176ed5a3612d465756a10576c0ce57edf55afa585f33af170d914613</citedby><cites>FETCH-LOGICAL-c557t-2a4e1c50d176ed5a3612d465756a10576c0ce57edf55afa585f33af170d914613</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0092-8674(00)80784-9$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10380924$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rocheleau, Christian E</creatorcontrib><creatorcontrib>Yasuda, Jun</creatorcontrib><creatorcontrib>Shin, Tae Ho</creatorcontrib><creatorcontrib>Lin, Rueyling</creatorcontrib><creatorcontrib>Sawa, Hitoshi</creatorcontrib><creatorcontrib>Okano, Hideyuki</creatorcontrib><creatorcontrib>Priess, James R</creatorcontrib><creatorcontrib>Davis, Roger J</creatorcontrib><creatorcontrib>Mello, Craig C</creatorcontrib><title>WRM-1 Activates the LIT-1 Protein Kinase to Transduce Anterior/Posterior Polarity Signals in C. elegans</title><title>Cell</title><addtitle>Cell</addtitle><description>During
C. elegans development, Wnt/WG signaling is required for differences in cell fate between sister cells born from anterior/posterior divisions. A β-catenin-related gene,
wrm-1, and the
lit-1 gene are effectors of this signaling pathway and appear to downregulate the activity of POP-1, a TCF/LEF–related protein, in posterior daughter cells. We show here that
lit-1 encodes a serine/threonine protein kinase homolog related to the
Drosophila tissue polarity protein Nemo. We demonstrate that the WRM-1 protein binds to LIT-1 in vivo and that WRM-1 can activate the LIT-1 protein kinase when coexpressed in vertebrate tissue culture cells. This activation leads to phosphorylation of POP-1 and to apparent changes in its subcellular localization. Our findings provide evidence for novel regulatory avenues for an evolutionarily conserved Wnt/WG signaling pathway.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>beta Catenin</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins</subject><subject>COS Cells</subject><subject>Cytoskeletal Proteins - genetics</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila</subject><subject>Enzyme Activation</subject><subject>Helminth Proteins - genetics</subject><subject>Helminth Proteins - metabolism</subject><subject>High Mobility Group Proteins - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mitogen-Activated Protein Kinases</subject><subject>Molecular Sequence Data</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Signal Transduction</subject><subject>Trans-Activators</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9PGzEQxa0KVALtR6DyCcFhwzi7tndPKIr6BxHUqKTq0TL2bGq0WQfbQcq3x2GjqjdOM5r5vRnpPULOGYwZMHH9ANBMilrI6hLgqgZZV0XzgYwYNLKomJwckdE_5IScxvgEADXn_CM5YVDWeVeNyOrPr_uC0alJ7kUnjDT9RTq_XebZIviErqd3rtcRafJ0GXQf7dYgnfYJg_PheuHj0NGF73RwaUcf3KrXXaRZOhtT7HCVVZ_IcZuH-PlQz8jvb1-Xsx_F_Of329l0XhjOZSomukJmOFgmBVquS8EmthJccqEZcCkMGOQSbcu5bjWveVuWumUSbMMqwcozcjHc3QT_vMWY1NpFg12ne_TbqERTV0wAvAtmBzMr9iAfQBN8jAFbtQlurcNOMVD7KNRbFGrvswJQb1GoJuu-HB5sH9do_1MN3mfgZgAw-_HiMKhoHPYGrQtokrLevfPiFabwlv8</recordid><startdate>19990611</startdate><enddate>19990611</enddate><creator>Rocheleau, Christian E</creator><creator>Yasuda, Jun</creator><creator>Shin, Tae Ho</creator><creator>Lin, Rueyling</creator><creator>Sawa, Hitoshi</creator><creator>Okano, Hideyuki</creator><creator>Priess, James R</creator><creator>Davis, Roger J</creator><creator>Mello, Craig C</creator><general>Elsevier Inc</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19990611</creationdate><title>WRM-1 Activates the LIT-1 Protein Kinase to Transduce Anterior/Posterior Polarity Signals in C. elegans</title><author>Rocheleau, Christian E ; Yasuda, Jun ; Shin, Tae Ho ; Lin, Rueyling ; Sawa, Hitoshi ; Okano, Hideyuki ; Priess, James R ; Davis, Roger J ; Mello, Craig C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-2a4e1c50d176ed5a3612d465756a10576c0ce57edf55afa585f33af170d914613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>beta Catenin</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>Caenorhabditis elegans Proteins</topic><topic>COS Cells</topic><topic>Cytoskeletal Proteins - genetics</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila</topic><topic>Enzyme Activation</topic><topic>Helminth Proteins - genetics</topic><topic>Helminth Proteins - metabolism</topic><topic>High Mobility Group Proteins - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mitogen-Activated Protein Kinases</topic><topic>Molecular Sequence Data</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Signal Transduction</topic><topic>Trans-Activators</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rocheleau, Christian E</creatorcontrib><creatorcontrib>Yasuda, Jun</creatorcontrib><creatorcontrib>Shin, Tae Ho</creatorcontrib><creatorcontrib>Lin, Rueyling</creatorcontrib><creatorcontrib>Sawa, Hitoshi</creatorcontrib><creatorcontrib>Okano, Hideyuki</creatorcontrib><creatorcontrib>Priess, James R</creatorcontrib><creatorcontrib>Davis, Roger J</creatorcontrib><creatorcontrib>Mello, Craig C</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rocheleau, Christian E</au><au>Yasuda, Jun</au><au>Shin, Tae Ho</au><au>Lin, Rueyling</au><au>Sawa, Hitoshi</au><au>Okano, Hideyuki</au><au>Priess, James R</au><au>Davis, Roger J</au><au>Mello, Craig C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>WRM-1 Activates the LIT-1 Protein Kinase to Transduce Anterior/Posterior Polarity Signals in C. elegans</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1999-06-11</date><risdate>1999</risdate><volume>97</volume><issue>6</issue><spage>717</spage><epage>726</epage><pages>717-726</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>During
C. elegans development, Wnt/WG signaling is required for differences in cell fate between sister cells born from anterior/posterior divisions. A β-catenin-related gene,
wrm-1, and the
lit-1 gene are effectors of this signaling pathway and appear to downregulate the activity of POP-1, a TCF/LEF–related protein, in posterior daughter cells. We show here that
lit-1 encodes a serine/threonine protein kinase homolog related to the
Drosophila tissue polarity protein Nemo. We demonstrate that the WRM-1 protein binds to LIT-1 in vivo and that WRM-1 can activate the LIT-1 protein kinase when coexpressed in vertebrate tissue culture cells. This activation leads to phosphorylation of POP-1 and to apparent changes in its subcellular localization. Our findings provide evidence for novel regulatory avenues for an evolutionarily conserved Wnt/WG signaling pathway.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10380924</pmid><doi>10.1016/S0092-8674(00)80784-9</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals beta Catenin Caenorhabditis elegans Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins COS Cells Cytoskeletal Proteins - genetics Cytoskeletal Proteins - metabolism DNA-Binding Proteins - metabolism Drosophila Enzyme Activation Helminth Proteins - genetics Helminth Proteins - metabolism High Mobility Group Proteins - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Mitogen-Activated Protein Kinases Molecular Sequence Data Phosphorylation Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Signal Transduction Trans-Activators |
| title | WRM-1 Activates the LIT-1 Protein Kinase to Transduce Anterior/Posterior Polarity Signals in C. elegans |
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