WRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior polarity signals in C. elegans
dc.contributor.author | Rocheleau, Christian Ernest | |
dc.contributor.author | Yasuda, Jun | |
dc.contributor.author | Shin, Tae Ho | |
dc.contributor.author | Lin, Rueyling | |
dc.contributor.author | Sawa, Hitoshi | |
dc.contributor.author | Okano, Hideyuki | |
dc.contributor.author | Priess, James R. | |
dc.contributor.author | Davis, Roger J. | |
dc.contributor.author | Mello, Craig C. | |
dc.date | 2022-08-11T08:08:47.000 | |
dc.date.accessioned | 2022-08-23T16:08:26Z | |
dc.date.available | 2022-08-23T16:08:26Z | |
dc.date.issued | 1999-06-25 | |
dc.date.submitted | 2008-12-08 | |
dc.identifier.citation | <p>Cell. 1999 Jun 11;97(6):717-26.</p> | |
dc.identifier.issn | 0092-8674 (Print) | |
dc.identifier.doi | 10.1016/S0092-8674(00)80784-9 | |
dc.identifier.pmid | 10380924 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/32446 | |
dc.description.abstract | During C. elegans development, Wnt/WG signaling is required for differences in cell fate between sister cells born from anterior/posterior divisions. A beta-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. | |
dc.language.iso | en_US | |
dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=10380924&dopt=Abstract">Link to Article in PubMed</a></p> | |
dc.relation.url | https://doi.org/10.1016/S0092-8674(00)80784-9 | |
dc.subject | Amino Acid Sequence; Animals; COS Cells; Caenorhabditis elegans; *Caenorhabditis elegans Proteins; Cytoskeletal Proteins; DNA-Binding Proteins; Enzyme Activation; Helminth Proteins; High Mobility Group Proteins; Membrane Proteins; *Mitogen-Activated Protein Kinases; Molecular Sequence Data; Phosphorylation; Protein-Serine-Threonine Kinases; *Signal Transduction; *Trans-Activators; beta Catenin | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | WRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior polarity signals in C. elegans | |
dc.type | Journal Article | |
dc.source.journaltitle | Cell | |
dc.source.volume | 97 | |
dc.source.issue | 6 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/1015 | |
dc.identifier.contextkey | 677733 | |
html.description.abstract | <p>During C. elegans development, Wnt/WG signaling is required for differences in cell fate between sister cells born from anterior/posterior divisions. A beta-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.</p> | |
dc.identifier.submissionpath | gsbs_sp/1015 | |
dc.contributor.department | Program in Molecular Medicine | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 717-26 |