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dc.contributor.authorRocheleau, Christian Ernest
dc.contributor.authorYasuda, Jun
dc.contributor.authorShin, Tae Ho
dc.contributor.authorLin, Rueyling
dc.contributor.authorSawa, Hitoshi
dc.contributor.authorOkano, Hideyuki
dc.contributor.authorPriess, James R.
dc.contributor.authorDavis, Roger J.
dc.contributor.authorMello, Craig C.
dc.date2022-08-11T08:08:47.000
dc.date.accessioned2022-08-23T16:08:26Z
dc.date.available2022-08-23T16:08:26Z
dc.date.issued1999-06-25
dc.date.submitted2008-12-08
dc.identifier.citation<p>Cell. 1999 Jun 11;97(6):717-26.</p>
dc.identifier.issn0092-8674 (Print)
dc.identifier.doi10.1016/S0092-8674(00)80784-9
dc.identifier.pmid10380924
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32446
dc.description.abstractDuring 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.isoen_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.urlhttps://doi.org/10.1016/S0092-8674(00)80784-9
dc.subjectAmino 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.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleWRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior polarity signals in C. elegans
dc.typeJournal Article
dc.source.journaltitleCell
dc.source.volume97
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1015
dc.identifier.contextkey677733
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.submissionpathgsbs_sp/1015
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages717-26


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