Quantifying the intra-regional precipitation variability in northwestern China over the past 1,400 years

There has been a surge of paleo-climatic/environmental studies of Northwestern China (NW China), a region characterized by a diverse assortment of hydro-climatic systems. Their common approach, however, focuses on "deducing regional resemblance" rather than "exploring regional variance." To date, efforts to produce a quantitative assessment of long-term intra-regional precipitation variability (IRPV) in NW China has been inadequate. In the present study, we base on historical flood/drought records to compile a decadal IRPV index for NW China spanned AD580-1979 and to find its major determinants via wavelet analysis. Results show that our IRPV index captures the footprints of internal hydro-climatic disparity in NW China. In addition, we find distinct similar to 120-200 year periodicities in the IRPV index over the Little Ice Age, which are attributable to the change of hydro-climatic influence of ocean-atmospheric modes during the period. Also, we offer statistical evidence of El Nino Southern Oscillation (Indo-Pacific warm pool sea surface temperature and China-wide land surface temperature) as the prominent multi-decadal to centennial (centennial to multi-centennial) determinant of the IRPV in NW China. The present study contributes to the quantitative validation of the long-term IRPV in NW China and its driving forces, covering the periods with and without instrumental records. It may help to comprehend the complex hydro-climatic regimes in the region.published_or_final_versio

Phosphoregulation of Ire1 RNase splicing activity.

Abstract Ire1 is activated in response to accumulation of misfolded proteins within the endoplasmic reticulum as part of the unfolded protein response (UPR). It is a unique enzyme, possessing both kinase and RNase activity that is required for specific splicing of Xbp1 mRNA leading to UPR activation. How phosphorylation impacts on the Ire1 splicing activity is unclear. In this study, we isolate distinct phosphorylated species of Ire1 and assess their effects on RNase splicing both in vitro and in vivo. We find that phosphorylation within the kinase activation loop significantly increases RNase splicing in vitro. Correspondingly, mutants of Ire1 that cannot be phosphorylated on the activation loop show decreased specific Xbp1 and promiscuous RNase splicing activity relative to wild-type Ire1 in cells. These data couple the kinase phosphorylation reaction to the activation state of the RNase, suggesting that phosphorylation of the activation loop is an important step in Ire1-mediated UPR activation.</jats:p