Sustainability of Global Golden Inland Waterways

Sustainable inland waterways should meet the needs of navigation without compromising the health of riverine ecosystems. Here we propose a hierarchical model to describe sustainable development of the Golden Inland Waterways (GIWs) which are characterized by great bearing capacity and transport need. Based on datasets from 66 large rivers (basin area > 100,000 km2) worldwide, we identify 34 GIWs, mostly distributed in Asia, Europe, North America, and South America, typically following a three-stage development path from the initial, through to the developing and on to the developed stage. For most GIWs, the exploitation ratio, defined as the ratio of actual to idealized bearing capacity, should be less than 80% due to ecological considerations. Combined with the indices of regional development, GIWs exploitation, and riverine ecosystem, we reveal the global diversity and evolution of GIWs' sustainability from 2015 to 2050, which highlights the importance of river-specific strategies for waterway exploitation worldwide

Selective Phosphorylation Modulates the PIP2 Sensitivity of the CaM-SK Channel Complex

Phosphatidylinositol bisphosphate (PIP2) regulates the activities of many membrane proteins including ion channels through direct interactions. However, the affinity of PIP2 is so high for some channel proteins that its physiological role as a modulator has been questioned. Here we show that PIP2 is an important cofactor for activation of small conductance Ca2+-activated potassium channels (SK) by Ca2+-bound calmodulin (CaM). Removal of the endogenous PIP2 inhibits SK channels. The PIP2-binding site resides at the interface of CaM and the SK C-terminus. We further demonstrate that the affinity of PIP2 for its target proteins can be regulated by cellular signaling. Phosphorylation of CaM T79, located adjacent to the PIP2-binding site, by Casein Kinase 2 reduces the affinity of PIP2 for the CaM-SK channel complex by altering the dynamic interactions among amino acid residues surrounding the PIP2-binding site. This effect of CaM phosphorylation promotes greater channel inhibition by G-protein-mediated hydrolysis of PIP2