@misc{toroser_huber_2000, title={Carbon and nitrogen metabolism and reversible protein phosphorylation}, volume={32}, ISBN={["0-12-005932-0"]}, ISSN={["2162-5948"]}, DOI={10.1016/S0065-2296(00)32032-8}, abstractNote={Publisher Summary This chapter focuses on the regulation of activity of several enzymes involved in carbon- and nitrogen-metabolisms that are phosphorylated by either calmodulin-like domain protein kinases (CDPKs) or sucrose nonfermenting-1 (SNF1)-related protein. Coordination between carbohydrate metabolism and nitrogen assimilation is essential to avoid direct competition, and it potentially involves control at several levels including gene expression, membrane transport, and enzyme activity. One important mechanism that may impact all three levels is reversible protein phosphorylation. Recent studies have also identified several other enzymes, including trehalose-6-phosphate synthase and glutamine synthetases, as phosphoproteins because they interact with 14-3-3 proteins in a phosphorylation-dependent manner. Several transport activities that may impact metabolism either directly or indirectly may also be controlled by phosphorylation. Of particular importance is the possible regulation by phosphorylation of ion and solute transport, for example, the plasma membrane H + -adenosine triphosphate (ATP)ase, plasma membrane K + channel, and the sucrose transporter.}, journal={ADVANCES IN BOTANICAL RESEARCH INCORPORATING ADVANCES IN PLANT PATHOLOGY, VOL 32}, author={Toroser, D and Huber, SC}, year={2000}, pages={435–458} }
 @article{toroser_plaut_huber_2000, title={Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate}, volume={123}, ISSN={["0032-0889"]}, DOI={10.1104/pp.123.1.403}, abstractNote={Abstract}, number={1}, journal={PLANT PHYSIOLOGY}, author={Toroser, D and Plaut, Z and Huber, SC}, year={2000}, month={May}, pages={403–411} }
 @article{toroser_mcmichael_krause_kurreck_sonnewald_stitt_huber_1999, title={Site-directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose-phosphate synthase modulation}, volume={17}, ISSN={["0960-7412"]}, DOI={10.1046/j.1365-313X.1999.00389.x}, abstractNote={Summary}, number={4}, journal={PLANT JOURNAL}, author={Toroser, D and McMichael, R and Krause, KP and Kurreck, J and Sonnewald, U and Stitt, M and Huber, SC}, year={1999}, month={Feb}, pages={407–413} }
 @article{toroser_huber_1998, title={3-hydroxy-3-methylglutaryl-coenzyme a reductase kinase and sucrose-phosphate synthase kinase activities in cauliflower florets: Ca2+ dependence and substrate specificities}, volume={355}, ISSN={["0003-9861"]}, DOI={10.1006/abbi.1998.0740}, abstractNote={Plant 3-hydroxy-3-methylglutaryl-CoA reductase(HMGR; EC 1.1.1.34) and sucrose-phosphate synthase (SPS; EC 2.4.1.14) and synthetic peptides designed from the known phosphorylation sites of plant HMGR (SAMS*: KSHMKYNRSTKDVK), rat acetyl-CoA carboxylase (SAMS: HMRSAMSGLHLVKRR), spinach SPS (SP2: GRRJRRISSVEJJDKK), and spinach NADH:nitrate reductase (NR6: GPTLKRTASTPFJNTTSK) were used to characterize kinase activities from cauliflower (Brassica oleracea L. ) inflorescences. The three major peaks of protein kinase activity resolved by anion-exchange FPLC are homologs of those observed previously in spinach leaves and thus are designated PKI, PKIV, and PKIII, listed in order of elution. PKIV was the most active in terms of phosphorylation and inactivation of recombinant Nicotiana HMGR and was also strictly Ca2+ dependent. The novel aspects are that PKIII has not been detected in previous cauliflower studies, that SAMS* is a more specific peptide substrate to identify potential HMGR kinases, and that the major HMGR kinase in cauliflower is Ca2+ dependent. Of the three major kinases that phosphorylated the SP2 peptide only PKI (partially Ca2+ sensitive) and PKIII (Ca2+ insensitive) inactivated native spinach leaf SPS. Cauliflower extracts contained endogenous SPS that was inactivated by endogenous kinase(s) in an ATP-dependent manner and this may be one of the substrate target proteins for PKI and/or PKIII. The substrate specificity of the three kinase peaks was studied using synthetic peptide variants of the SP2 sequence. All three kinases had a strong preference for peptides with a basic residue at P-6 (as in SP2 and SAMS*; SAMS has a free amino terminus at this position) or a Pro at P-7 (as in NR6). This requirement for certain residues at P-6 or P-7 was not recognized in earlier studies but appears to be a general requirement. In plant HMGR, a conserved His residue at P-6 is involved directly in catalysis and this may explain why substrates reduced HMGR phosphorylation in vitro.}, number={2}, journal={ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS}, author={Toroser, D and Huber, SC}, year={1998}, month={Jul}, pages={291–300} }
 @article{toroser_athwal_huber_1998, title={Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins}, volume={435}, ISSN={["0014-5793"]}, DOI={10.1016/S0014-5793(98)01048-5}, abstractNote={We report an Mg2+‐dependent interaction between spinach leaf sucrose‐phosphate synthase (SPS) and endogenous 14‐3‐3 proteins, as evidenced by co‐elution during gel filtration and co‐immunoprecipitation. The content of 14‐3‐3s associated with an SPS immunoprecipitate was inversely related to activity, and was specifically reduced when tissue was pretreated with 5‐aminoimidazole‐4‐carboxamide riboside, suggesting metabolite control in vivo. A synthetic phosphopeptide based on Ser‐229 was shown by surface plasmon resonance to bind a recombinant plant 14‐3‐3, and addition of the phosphorylated SPS‐229 peptide was found to stimulate the SPS activity of an SPS:14‐3‐3 complex. Taken together, the results suggest a regulatory interaction of 14‐3‐3 proteins with Ser‐229 of SPS.}, number={1}, journal={FEBS LETTERS}, author={Toroser, D and Athwal, GS and Huber, SC}, year={1998}, month={Sep}, pages={110–114} }
 @article{toroser_huber_1997, title={Protein phosphorylation as a mechanism for osmotic-stress activation of sucrose-phosphate synthase in spinach leaves}, volume={114}, ISSN={["0032-0889"]}, DOI={10.1104/pp.114.3.947}, abstractNote={Abstract}, number={3}, journal={PLANT PHYSIOLOGY}, author={Toroser, D and Huber, SC}, year={1997}, month={Jul}, pages={947–955} }