Identification and Functional Role of Myo-Inositol Polyphosphate 5-Phosphatase Protein Complexes

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dc.contributor.authorAnanieva-Stoyanova, Elitsa Antonovaen
dc.contributor.committeechairGillaspy, Glenda E.en
dc.contributor.committeememberTholl, Dorotheaen
dc.contributor.committeememberTu, Zhijian Jakeen
dc.contributor.committeememberSitz, Thomas O.en
dc.contributor.departmentBiochemistryen
dc.date.accessioned2014-03-14T20:12:59Zen
dc.date.adate2009-06-25en
dc.date.available2014-03-14T20:12:59Zen
dc.date.issued2009-06-08en
dc.date.rdate2012-03-27en
dc.date.sdate2009-06-12en
dc.description.abstractTo survive, an organism must constantly adjust its internal state to changes in the environment from which it receives signals. The signals set off a chain of events referred to signal transduction. Signal transduction systems are especially important in multicellular organisms, such as plants and animals, because of the need to coordinate the activities of hundreds to trillions of cells. Plants, in particular, have a special need for perceiving signals from their environment because of their static nature. As in the animal cell, the first steps in perception of a signal include signal interaction with a receptor, signal amplification through second messenger production, and signal termination through second messenger hydrolysis. Myo-inositol polyphosphate 5-phosphatases (5PTases) (EC 3.1.3.56) have unique signal terminating abilities toward the second messenger inositol trisphosphate (Ins (1,4,5)P3, InsP3). In Arabidopsis thaliana there are 15 members of the 5PTase family, the majority of which contain a single 5PTase catalytic domain. Four members of the Arabidopsis 5PTase family, however, have a unique protein domain structure, with additional N-terminal WD40 repeats that are implicated in protein-protein interactions. The research presented here focused on the identification of 5PTase interacting proteins and the characterization of their functional role in Arabidopsis. To accomplish this goal, I examined a 5PTase13-interacting protein, the sucrose (Suc) nonfermenting-1-related kinase, SnRK1.1, an important energy sensor that is highly conserved among eukaryotes. My identification of a 5PTase13:SnRK1.1 complex points to the novel interaction of this metabolic modulator and inositol signaling/metabolism. 5PTase13 , however, plays a regulatory role in other plant specific processes as well, since I also identified the Arabidopsis homolog (Atp80) of the human WDR48 (HsWDR48, Hsp80) as a novel protein interactor of 5PTase13. My results indicate that Atp80 is important for leaf emergence, development and senescence likely via a regulatory interaction with 5PTase13 and PINOID â binding protein (PBP1).en
dc.description.degreePh. D.en
dc.identifier.otheretd-06122009-111248en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-06122009-111248/en
dc.identifier.urihttp://hdl.handle.net/10919/28028en
dc.publisherVirginia Techen
dc.relation.haspartDissertation.pdfen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectmyo-inositol polyphosphate 5-phosphataseen
dc.subjectsucrose nonfermenting-1-related kinaseen
dc.subjectArabidopsis thalianaen
dc.subjectinositol trisphosphate [Ins(1,4,5)P₃]en
dc.subjectarabidopsis homolog of p80en
dc.titleIdentification and Functional Role of Myo-Inositol Polyphosphate 5-Phosphatase Protein Complexesen
dc.typeDissertationen
thesis.degree.disciplineBiochemistryen
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen
thesis.degree.leveldoctoralen
thesis.degree.namePh. D.en

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