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dc.contributor.authorGuertin, David A.
dc.contributor.authorMcCollum, Dannel
dc.date2022-08-11T08:08:58.000
dc.date.accessioned2022-08-23T16:14:07Z
dc.date.available2022-08-23T16:14:07Z
dc.date.issued2001-06-01
dc.date.submitted2008-09-23
dc.identifier.citationJ Biol Chem. 2001 Jul 27;276(30):28185-9. Epub 2001 May 30. <a href="http://dx.doi.org/10.1074/jbc.M103802200">Link to article on publisher's site</a>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.M103802200
dc.identifier.pmid11384993
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33787
dc.description.abstractSid1p is a group II p21-activated kinase/germinal center kinase family member that is part of a signaling network required for cytokinesis in fission yeast. Germinal center kinases are characterized by well conserved amino-terminal catalytic domains followed by less conserved carboxyl termini. The carboxyl termini among group I germinal center kinases are moderately conserved and thought to be regulatory regions. Little is known about the carboxyl termini of group II family members. Sid1p has been shown to bind the novel protein Cdc14p; however, the functional significance of this interaction is unknown. Here we report that the carboxyl terminus of Sid1p is an essential regulatory region. Our results indicate that this region contains the binding domain for Cdc14p, and this association is required for full Sid1p catalytic activity as well as intracellular localization. Furthermore, overexpression of the carboxyl terminus of Sid1p alone compromises the signaling of cytokinesis. We conclude that Cdc14p positively regulates the Sid1p kinase by binding the noncatalytic carboxyl-terminal region of the protein.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11384993&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1074/jbc.M103802200
dc.subjectAlleles; Catalysis; Catalytic Domain; Cell Cycle Proteins; Electrophoresis, Polyacrylamide Gel; Green Fluorescent Proteins; Immunoblotting; Luminescent Proteins; Microscopy, Fluorescence; Mutation; Phosphotransferases; Plasmids; Precipitin Tests; Protein Binding; Protein Biosynthesis; Protein Kinases; Protein Structure, Tertiary; *Protein Tyrosine Phosphatases; Recombinant Fusion Proteins; *Saccharomyces cerevisiae Proteins; Schizosaccharomyces; Structure-Activity Relationship; Temperature; Transcription, Genetic
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleInteraction between the noncatalytic region of Sid1p kinase and Cdc14p is required for full catalytic activity and localization of Sid1p
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume276
dc.source.issue30
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/449
dc.identifier.contextkey635944
html.description.abstract<p>Sid1p is a group II p21-activated kinase/germinal center kinase family member that is part of a signaling network required for cytokinesis in fission yeast. Germinal center kinases are characterized by well conserved amino-terminal catalytic domains followed by less conserved carboxyl termini. The carboxyl termini among group I germinal center kinases are moderately conserved and thought to be regulatory regions. Little is known about the carboxyl termini of group II family members. Sid1p has been shown to bind the novel protein Cdc14p; however, the functional significance of this interaction is unknown. Here we report that the carboxyl terminus of Sid1p is an essential regulatory region. Our results indicate that this region contains the binding domain for Cdc14p, and this association is required for full Sid1p catalytic activity as well as intracellular localization. Furthermore, overexpression of the carboxyl terminus of Sid1p alone compromises the signaling of cytokinesis. We conclude that Cdc14p positively regulates the Sid1p kinase by binding the noncatalytic carboxyl-terminal region of the protein.</p>
dc.identifier.submissionpathgsbs_sp/449
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages28185-9


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