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dc.contributor.authorShin, Tae Ho
dc.contributor.authorYasuda, Jun
dc.contributor.authorRocheleau, Christian Ernest
dc.contributor.authorLin, Rueyling
dc.contributor.authorSoto, Martha C.
dc.contributor.authorBei, Yanxia
dc.contributor.authorDavis, Roger J.
dc.contributor.authorMello, Craig C.
dc.date2022-08-11T08:08:48.000
dc.date.accessioned2022-08-23T16:08:50Z
dc.date.available2022-08-23T16:08:50Z
dc.date.issued1999-09-17
dc.date.submitted2008-12-11
dc.identifier.citation<p>Mol Cell. 1999 Aug;4(2):275-80.</p>
dc.identifier.issn1097-2765 (Print)
dc.identifier.doi10.1016/S1097-2765(00)80375-5
dc.identifier.pmid10488343
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32544
dc.description.abstractIn C. elegans, a Wnt/WG-like signaling pathway down-regulates the TCF/LEF-related protein, POP-1, to specify posterior cell fates. Effectors of this signaling pathway include a beta-catenin homolog, WRM-1, and a conserved protein kinase, LIT-1. WRM-1 and LIT-1 form a kinase complex that can directly phosphorylate POP-1, but how signaling activates WRM-1/LIT-1 kinase is not yet known. Here we show that mom-4, a genetically defined effector of polarity signaling, encodes a MAP kinase kinase kinase-related protein that stimulates the WRM-1/LIT-1-dependent phosphorylation of POP-1. LIT-1 kinase activity requires a conserved residue analogous to an activating phosphorylation site in other kinases, including MAP kinases. These findings suggest that anterior/posterior polarity signaling in C. elegans may involve a MAP kinase-like signaling mechanism.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=10488343&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1016/S1097-2765(00)80375-5
dc.subjectAmino Acid Sequence; Animals; Body Patterning; Caenorhabditis elegans; *Caenorhabditis elegans Proteins; Conserved Sequence; Cytoskeletal Proteins; DNA-Binding Proteins; Embryo, Nonmammalian; Endoderm; Enzyme Activation; Helminth Proteins; High Mobility Group Proteins; Membrane Proteins; Molecular Sequence Data; Phosphorylation; Protein-Serine-Threonine Kinases; Sequence Alignment; Sequence Homology, Amino Acid; Signal Transduction; Transcription Factors
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMOM-4, a MAP kinase kinase kinase-related protein, activates WRM-1/LIT-1 kinase to transduce anterior/posterior polarity signals in C. elegans
dc.typeJournal Article
dc.source.journaltitleMolecular cell
dc.source.volume4
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1109
dc.identifier.contextkey680281
html.description.abstract<p>In C. elegans, a Wnt/WG-like signaling pathway down-regulates the TCF/LEF-related protein, POP-1, to specify posterior cell fates. Effectors of this signaling pathway include a beta-catenin homolog, WRM-1, and a conserved protein kinase, LIT-1. WRM-1 and LIT-1 form a kinase complex that can directly phosphorylate POP-1, but how signaling activates WRM-1/LIT-1 kinase is not yet known. Here we show that mom-4, a genetically defined effector of polarity signaling, encodes a MAP kinase kinase kinase-related protein that stimulates the WRM-1/LIT-1-dependent phosphorylation of POP-1. LIT-1 kinase activity requires a conserved residue analogous to an activating phosphorylation site in other kinases, including MAP kinases. These findings suggest that anterior/posterior polarity signaling in C. elegans may involve a MAP kinase-like signaling mechanism.</p>
dc.identifier.submissionpathgsbs_sp/1109
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages275-80


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