Foraging trip duration of honeybee increases during a poor air quality episode and the increase persists thereafter.

Increased concentration of airborne particulate matter (PM) in the atmosphere alters the degree of polarization of skylight which is used by honeybees for navigation during their foraging trips. However, little has empirically shown whether poor air quality indeed affects foraging performance (foraging trip duration) of honeybee. Here, we show apparent increases in the average duration of honeybee foraging during and after a heavy air pollution event compared with that of the pre-event period. The average foraging duration of honeybees during the event increased by 32 min compared with the pre-event conditions, indicating that 71% more time was spent on foraging. Moreover, the average foraging duration measured after the event did not recover to its pre-event level. We further investigated whether an optical property (Depolarization Ratio, DR) of dominant PM in the atmosphere and level of air pollution (fine PM mass concentration) affect foraging trip duration. The result demonstrates the DR and fine PM mass concentration have significant effects on honeybee foraging trip duration. Foraging trip duration increases with decreasing DR while it increases with increasing fine PM mass concentration. In addition, the effects of fine PM mass concentration are synergistic with overcast skies. Our study implies that poor air quality could pose a new threat to bee foraging.

TANK-Binding Kinase 1 Regulates the Localization of Acyl-CoA Synthetase ACSL1 to Control Hepatic Fatty Acid Oxidation.

Hepatic TANK (TRAF family member associated NFκB activator)-binding kinase 1 (TBK1) activity is increased during obesity, and administration of a TBK1 inhibitor reduces fatty liver. Surprisingly, liver-specific TBK1 knockout in mice produces fatty liver by reducing fatty acid oxidation. TBK1 functions as a scaffolding protein to localize acyl-CoA synthetase long-chain family member 1 (ACSL1) to mitochondria, which generates acyl-CoAs that are channeled for ß-oxidation. TBK1 is induced during fasting and maintained in the unphosphorylated, inactive state, enabling its high affinity binding to ACSL1 in mitochondria. In TBK1-deficient liver, ACSL1 is shifted to the endoplasmic reticulum to promote fatty acid re-esterification in lieu of oxidation in response to fasting, which accelerates hepatic lipid accumulation. The impaired fatty acid oxidation in TBK1-deficient hepatocytes is rescued by the expression of kinase-dead TBK1. Thus, TBK1 operates as a rheostat to direct the fate of fatty acids in hepatocytes, supporting oxidation when inactive during fasting and promoting re-esterification when activated during obesity.