The Par-1 family of serine/threonine protein kinases functions to regulate cell polarity and is conserved from yeast to humans. Par-1 is encoded by one of six Par: partitioning-defective) genes: Par-1-6) originally identified in a genetic screen conducted in Caenorhabditis elegans: C. elegans). The mammalian Par-1 family is comprised of four members: Par-1a, b, c and d). Par-1 kinases are regulated by two arms of the Protein Kinase C: PKC) pathway. Atypical Protein Kinase C: aPKC) phosphorylates Par-1b on a conserved threonine residue: T595) and I participated in studies demonstrating that novel Protein Kinase C: nPKC) activates Protein Kinase D: PKD) to directly phosphorylate Par-1b on serine 400: S400), a residue that is conserved in all four mammalian Par-1 kinases as well as the fly ortholog. Phosphorylation of Par-1b on T595 and S400 causes Par-1b to relocate from membranes to the cytosol and to bind 14-3-3 proteins. In 2004, Brajenovic, et al. reported the results of a study that used tandem affinity purification: TAP) to isolate human Par-1d along with associated proteins. Nrdp1/RNF41, a RING finger E3 ligase was identified in their screen along with 14-3-3 and aPKC. I found that Par-1b binds to RNF41 and I identified RNF41 as a novel cell polarity determinant. My work demonstrated that phosphorylation of RNF41 on S254 by Par-1b is necessary for establishing epithelial cell polarity.
","abstract_html":"<p>The Par-1 family of serine/threonine protein kinases functions to regulate cell polarity and is conserved from yeast to humans. Par-1 is encoded by one of six Par: partitioning-defective) genes: Par-1-6) originally identified in a genetic screen conducted in Caenorhabditis elegans: C. elegans). The mammalian Par-1 family is comprised of four members: Par-1a, b, c and d). Par-1 kinases are regulated by two arms of the Protein Kinase C: PKC) pathway. Atypical Protein Kinase C: aPKC) phosphorylates Par-1b on a conserved threonine residue: T595) and I participated in studies demonstrating that novel Protein Kinase C: nPKC) activates Protein Kinase D: PKD) to directly phosphorylate Par-1b on serine 400: S400), a residue that is conserved in all four mammalian Par-1 kinases as well as the fly ortholog. Phosphorylation of Par-1b on T595 and S400 causes Par-1b to relocate from membranes to the cytosol and to bind 14-3-3 proteins. In 2004, Brajenovic, et al. reported the results of a study that used tandem affinity purification: TAP) to isolate human Par-1d along with associated proteins. Nrdp1/RNF41, a RING finger E3 ligase was identified in their screen along with 14-3-3 and aPKC. I found that Par-1b binds to RNF41 and I identified RNF41 as a novel cell polarity determinant. My work demonstrated that phosphorylation of RNF41 on S254 by Par-1b is necessary for establishing epithelial cell polarity.</p>","abstract_has_math":false,"creators":["Vega, Katherine Terese"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biology and Biomedical Sciences: Biochemistry","degree_department":null,"school":null,"contributors":["Helen Piwnica-Worms"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012-09-01T07:00:00Z","date_published":"2012-09-01T07:00:00Z","updated_at":"2026-07-24T06:12:41Z","subjects":["cell polarity","Par-1b","phosphorylation","RNF41"],"languages":["English (en)"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.7936/K7KD1VW1"],"render_values":[{"text":"https://doi.org/10.7936/K7KD1VW1","href":"https://doi.org/10.7936/K7KD1VW1","code":true}]}]},"links":{"outbound_url":"https://openscholarship.wustl.edu/etd/985","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Helen Piwnica-Worms"]},{"key":"dc:creator","label":"Author","values":["Vega, Katherine Terese"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2014-01-07T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology and Biomedical Sciences: Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["cell polarity","Par-1b","phosphorylation","RNF41"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English (en)"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://openscholarship.wustl.edu/etd/985"]},{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.7936/K7KD1VW1"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The Par-1 family of serine/threonine protein kinases functions to regulate cell polarity and is conserved from yeast to humans. Par-1 is encoded by one of six Par: partitioning-defective) genes: Par-1-6) originally identified in a genetic screen conducted in Caenorhabditis elegans: C. elegans). The mammalian Par-1 family is comprised of four members: Par-1a, b, c and d). Par-1 kinases are regulated by two arms of the Protein Kinase C: PKC) pathway. Atypical Protein Kinase C: aPKC) phosphorylates Par-1b on a conserved threonine residue: T595) and I participated in studies demonstrating that novel Protein Kinase C: nPKC) activates Protein Kinase D: PKD) to directly phosphorylate Par-1b on serine 400: S400), a residue that is conserved in all four mammalian Par-1 kinases as well as the fly ortholog. Phosphorylation of Par-1b on T595 and S400 causes Par-1b to relocate from membranes to the cytosol and to bind 14-3-3 proteins. In 2004, Brajenovic, et al. reported the results of a study that used tandem affinity purification: TAP) to isolate human Par-1d along with associated proteins. Nrdp1/RNF41, a RING finger E3 ligase was identified in their screen along with 14-3-3 and aPKC. I found that Par-1b binds to RNF41 and I identified RNF41 as a novel cell polarity determinant. My work demonstrated that phosphorylation of RNF41 on S254 by Par-1b is necessary for establishing epithelial cell polarity.
"]},{"key":"dc:title","label":"Title","values":["Functional Interactions Between Par-1b Protein Kinase and RNF41 E3 Ubiquitin Ligase"]}]}],"canonical_facts":{"dc:contributor":["Helen Piwnica-Worms"],"dc:creator":["Vega, Katherine Terese"],"dc:date.available":["2014-01-07T08:00:00Z"],"dc:description.abstract":["The Par-1 family of serine/threonine protein kinases functions to regulate cell polarity and is conserved from yeast to humans. Par-1 is encoded by one of six Par: partitioning-defective) genes: Par-1-6) originally identified in a genetic screen conducted in Caenorhabditis elegans: C. elegans). The mammalian Par-1 family is comprised of four members: Par-1a, b, c and d). Par-1 kinases are regulated by two arms of the Protein Kinase C: PKC) pathway. Atypical Protein Kinase C: aPKC) phosphorylates Par-1b on a conserved threonine residue: T595) and I participated in studies demonstrating that novel Protein Kinase C: nPKC) activates Protein Kinase D: PKD) to directly phosphorylate Par-1b on serine 400: S400), a residue that is conserved in all four mammalian Par-1 kinases as well as the fly ortholog. Phosphorylation of Par-1b on T595 and S400 causes Par-1b to relocate from membranes to the cytosol and to bind 14-3-3 proteins. In 2004, Brajenovic, et al. reported the results of a study that used tandem affinity purification: TAP) to isolate human Par-1d along with associated proteins. Nrdp1/RNF41, a RING finger E3 ligase was identified in their screen along with 14-3-3 and aPKC. I found that Par-1b binds to RNF41 and I identified RNF41 as a novel cell polarity determinant. My work demonstrated that phosphorylation of RNF41 on S254 by Par-1b is necessary for establishing epithelial cell polarity.
"],"dc:identifier":["https://openscholarship.wustl.edu/etd/985"],"dc:identifier.doi":["https://doi.org/10.7936/K7KD1VW1"],"dc:language":["English (en)"],"dc:subject":["cell polarity","Par-1b","phosphorylation","RNF41"],"dc:title":["Functional Interactions Between Par-1b Protein Kinase and RNF41 E3 Ubiquitin Ligase"],"thesis:degree_discipline":["Biology and Biomedical Sciences: Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T06:12:41Z"}