Implications of future climate and atmospheric CO2 content for regional biogeochemistry,biogeography and ecosystem services across East Africa

We model future changes in land biogeochemistry and biogeography across East Africa. East Africa is one of few tropical regions where general circulation model (GCM) future climate projections exhibit a robust response of strong future warming and general annual‐mean rainfall increases. Eighteen future climate projections from nine GCMs participating in the Intergovernmental Panel on Climate Change (IPCC) Fourth Assessment were used as input to the LPJ dynamic global vegetation model (DGVM), which predicted vegetation patterns and carbon storage in agreement with satellite observations and forest inventory data under the present‐day climate. All simulations showed future increases in tropical woody vegetation over the region at the expense of grasslands. Regional increases in net primary productivity (NPP) (18–36%) and total carbon storage (3–13%) by 2080–2099 compared with the present‐day were common to all simulations. Despite decreases in soil carbon after 2050, seven out of nine simulations continued to show an annual net land carbon sink in the final decades of the 21st century because vegetation biomass continued to increase. The seasonal cycles of rainfall and soil moisture show future increases in wet season rainfall across the GCMs with generally little change in dry season rainfall. Based on the simulated present‐day climate and its future trends, the GCMs can be grouped into four broad categories. Overall, our model results suggest that East Africa, a populous and economically poor region, is likely to experience some ecosystem service benefits through increased precipitation, river runoff and fresh water availability. Resulting enhancements in NPP may lead to improved crop yields in some areas. Our results stand in partial contradiction to other studies that suggest possible negative consequences for agriculture, biodiversity and other ecosystem services caused by temperature increases.     

The Full-Length, Cytoplasmic C-Terminus of the β2-Adrenergic Receptor Expressed in E. coli Acts as a Substrate for Phosphorylation by Protein Kinase A, Insulin Receptor Tyrosine Kinase, GRK2, but Not Protein Kinase C and Suppresses Desensitization when Expressed in Vivo

The ability of the cytoplasmic, full-length C-terminus of the β2-adrenergic receptor (BAC1) expressed in Escherichia coli to act as a functional domain and substrate for protein phosphorylation was tested. BAC1 was expressed at high-levels, purified, and examined in solution as a substrate for protein phosphorylation. The mobility of BAC1 on SDS–PAGE mimics that of the native receptor itself, displaying decreased mobility upon chemical reduction of disulfide bonds. Importantly, the C-terminal, cytoplasmic domain of the receptor expressed in E. coli was determined to be a substrate for phosphorylation by several candidate protein kinases known to regulate G-protein-linked receptors. Mapping was performed by proteolytic degradation and matrix-assisted laser desorption ionization, time-of-flight mass spectrometry. Purified BAC1 is phosphorylated readily by protein kinase A, the phosphorylation occurring within the predicted motif RRSSSK. The kinetic properties of the phosphorylation by protein kinase A displayed cooperative character. The activated insulin receptor tyrosine kinase, which phosphorylates the beta-adrenergic receptor in vivo, phosphorylates BAC1. The Y364 residue of BAC1 was predominantly phosphorylated by the insulin receptor kinase. GRK2 catalyzed modest phosphorylation of BAC1. Phosphorylation of the human analog of BAC1 in which Cys341 and Cys378 were mutated to minimize disulfide bonding constraints, displayed robust phosphorylation following thermal activation, suggesting under standard conditions that the population of BAC1 molecules capable of assuming the “activated” conformer required by GRKs is low. BAC1 was not a substrate for protein kinase C, suggesting that the canonical site in the second cytoplasmic loop of the intact receptor is preferred. The functional nature of BAC1 was tested additionally by expression of BAC1 protein in human epidermoid carcinoma A431 cells. BAC1 was found to act as a dominant-negative, blocking agonist-induced desensitization of the beta-adrenergic receptor when expressed in mammalian cells. Thus, the C-terminal, cytoplasmic tail of this G-protein-linked receptor expressed in E. coli acts as a functional domain, displaying fidelity with regard to protein kinase action in vivo and acting as a dominant-negative with respect to agonist-induced desensitization.