{"id":{"repo_id":"guelph","oai_identifier":"oai:atrium.lib.uoguelph.ca:10214/23753"},"canonical_url":"https://search.dev.ndltd.org/etd/guelph/oai:atrium.lib.uoguelph.ca:10214/23753","repository":{"repo_id":"guelph","name":"University of Guelph","base_url":"https://atrium.lib.uoguelph.ca/server/oai/request"},"display":{"title":"A Regulatory Role for 14-3-3 Proteins in the Starch Biosynthetic Pathway of Zea mays","abstract":"Starch derived from cereal endosperm is responsible for supporting humanity’s global caloric requirements and is applied in various industrial applications. Semi-crystalline starch granules are comprised of glucose polymers, amylose and amylopectin, which are synthesized by four classes of enzymes including ADP-glucose pyrophosphorylase (AGPase), starch synthases (SS), starch branching enzymes (SBE), and starch debranching enzymes (DBE). Several SS and SBE isoforms form large phosphorylation-dependent heteromeric protein complexes. A class of eukaryotic proteins called “14-3-3” dimerize and interact with phosphorylated clients to regulate enzymatic activity, localization and protein interactions. A series of bioinformatic and biochemical techniques identified GF14-6 as the only detectable 14-3-3 isoform in maize amyloplasts. Recombinant GF14-6 was shown to interact with SSI, SBEIIa and SBEIIb in affinity bait assays. Reciprocal interactions using recombinant SBEIIb demonstrated phosphorylation-dependent interactions with endogenous 14-3-3s. These results point towards a regulatory role for 14-3-3 proteins regulating starch biosynthesis in maize endosperm.","abstract_html":"Starch derived from cereal endosperm is responsible for supporting humanity’s global caloric requirements and is applied in various industrial applications. Semi-crystalline starch granules are comprised of glucose polymers, amylose and amylopectin, which are synthesized by four classes of enzymes including ADP-glucose pyrophosphorylase (AGPase), starch synthases (SS), starch branching enzymes (SBE), and starch debranching enzymes (DBE). Several SS and SBE isoforms form large phosphorylation-dependent heteromeric protein complexes. A class of eukaryotic proteins called “14-3-3” dimerize and interact with phosphorylated clients to regulate enzymatic activity, localization and protein interactions. A series of bioinformatic and biochemical techniques identified GF14-6 as the only detectable 14-3-3 isoform in maize amyloplasts. Recombinant GF14-6 was shown to interact with SSI, SBEIIa and SBEIIb in affinity bait assays. Reciprocal interactions using recombinant SBEIIb demonstrated phosphorylation-dependent interactions with endogenous 14-3-3s. These results point towards a regulatory role for 14-3-3 proteins regulating starch biosynthesis in maize endosperm.","abstract_has_math":false,"creators":["Carswell, Matthew"],"institution":"University of Guelph","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Emes, Michael"],"committee_chairs":[],"committee_members":[],"year":null,"date_issued":"","date_published":null,"updated_at":"2026-08-21T16:45:07Z","subjects":["Starch","14-3-3","protein-protein interactions","phosphorylation"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/10214/23753","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"source_record":{"url":"https://atrium.lib.uoguelph.ca/server/oai/request?verb=GetRecord&metadataPrefix=dim&identifier=oai%3Aatrium.lib.uoguelph.ca%3A10214%2F23753","prefix":"dim"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Emes, Michael"]},{"key":"dc:creator","label":"Author","values":["Carswell, Matthew"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2021-01-13T21:17:56Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2021-01-13T21:17:56Z"]},{"key":"dc:publisher","label":"Institution","values":["University of Guelph"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Starch","14-3-3","protein-protein interactions","phosphorylation"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/10214/23753"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Starch derived from cereal endosperm is responsible for supporting humanity’s global caloric requirements and is applied in various industrial applications. Semi-crystalline starch granules are comprised of glucose polymers, amylose and amylopectin, which are synthesized by four classes of enzymes including ADP-glucose pyrophosphorylase (AGPase), starch synthases (SS), starch branching enzymes (SBE), and starch debranching enzymes (DBE). Several SS and SBE isoforms form large phosphorylation-dependent heteromeric protein complexes. A class of eukaryotic proteins called “14-3-3” dimerize and interact with phosphorylated clients to regulate enzymatic activity, localization and protein interactions. A series of bioinformatic and biochemical techniques identified GF14-6 as the only detectable 14-3-3 isoform in maize amyloplasts. Recombinant GF14-6 was shown to interact with SSI, SBEIIa and SBEIIb in affinity bait assays. Reciprocal interactions using recombinant SBEIIb demonstrated phosphorylation-dependent interactions with endogenous 14-3-3s. These results point towards a regulatory role for 14-3-3 proteins regulating starch biosynthesis in maize endosperm."]},{"key":"dc:title","label":"Title","values":["A Regulatory Role for 14-3-3 Proteins in the Starch Biosynthetic Pathway of Zea mays"]}]}],"canonical_facts":{"dc:contributor.advisor":["Emes, Michael"],"dc:creator":["Carswell, Matthew"],"dc:date.accessioned":["2021-01-13T21:17:56Z"],"dc:date.available":["2021-01-13T21:17:56Z"],"dc:description.abstract":["Starch derived from cereal endosperm is responsible for supporting humanity’s global caloric requirements and is applied in various industrial applications. Semi-crystalline starch granules are comprised of glucose polymers, amylose and amylopectin, which are synthesized by four classes of enzymes including ADP-glucose pyrophosphorylase (AGPase), starch synthases (SS), starch branching enzymes (SBE), and starch debranching enzymes (DBE). Several SS and SBE isoforms form large phosphorylation-dependent heteromeric protein complexes. A class of eukaryotic proteins called “14-3-3” dimerize and interact with phosphorylated clients to regulate enzymatic activity, localization and protein interactions. A series of bioinformatic and biochemical techniques identified GF14-6 as the only detectable 14-3-3 isoform in maize amyloplasts. Recombinant GF14-6 was shown to interact with SSI, SBEIIa and SBEIIb in affinity bait assays. Reciprocal interactions using recombinant SBEIIb demonstrated phosphorylation-dependent interactions with endogenous 14-3-3s. These results point towards a regulatory role for 14-3-3 proteins regulating starch biosynthesis in maize endosperm."],"dc:identifier.uri":["https://hdl.handle.net/10214/23753"],"dc:language.iso":["en"],"dc:publisher":["University of Guelph"],"dc:subject":["Starch","14-3-3","protein-protein interactions","phosphorylation"],"dc:title":["A Regulatory Role for 14-3-3 Proteins in the Starch Biosynthetic Pathway of Zea mays"],"dc:type":["Thesis"]},"updated_at":"2026-08-21T16:45:07Z"}