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The fabrication of plagioclase feldspar microdevices: an experimental tool for pore scale mineral dissolution studies 期刊论文
Water Resources Research, 2020
作者:  Heewon Jung;  Margariete Malenda;  Nathan Worts;  Jeff Squier;  Brian P. Gorman;  Alexis Navarre‐;  Sitchler
收藏  |  浏览/下载:4/0  |  提交时间:2020/08/18
Stable machine-learning parameterization of subgrid processes for climate modeling at a range of resolutions 期刊论文
NATURE COMMUNICATIONS, 2020, 11 (1)
作者:  Yuval, Janni;  39;Gorman, Paul A.
收藏  |  浏览/下载:4/0  |  提交时间:2020/07/06
Extreme rainfall events alter the trophic structure in bromeliad tanks across the Neotropics 期刊论文
NATURE COMMUNICATIONS, 2020, 11 (1)
作者:  Romero, Gustavo Q.;  39;Gorman, Eoin J.
收藏  |  浏览/下载:6/0  |  提交时间:2020/06/29
Weakening of the Extratropical Storm Tracks in Solar Geoengineering Scenarios 期刊论文
GEOPHYSICAL RESEARCH LETTERS, 2020, 47 (11)
作者:  Gertler, Charles G.;  39;Gorman, Paul A.
收藏  |  浏览/下载:5/0  |  提交时间:2020/05/13
Storm Tracks  Geoengineering  Available Potential Energy  Climate Change  Extratropical Cyclones  
An intestinal zinc sensor regulates food intake and developmental growth 期刊论文
NATURE, 2020, 580 (7802) : 263-+
作者:  Wu, Thomas D.;  39;Gorman, William E.
收藏  |  浏览/下载:14/0  |  提交时间:2020/07/03

Hodor, an intestinal zinc-gated chloride channel, controls systemic growth in Drosophila by promoting food intake and by modulating Tor signalling and lysosomal homeostasis within enterocytes.


In cells, organs and whole organisms, nutrient sensing is key to maintaining homeostasis and adapting to a fluctuating environment(1). In many animals, nutrient sensors are found within the enteroendocrine cells of the digestive system  however, less is known about nutrient sensing in their cellular siblings, the absorptive enterocytes(1). Here we use a genetic screen in Drosophila melanogaster to identify Hodor, an ionotropic receptor in enterocytes that sustains larval development, particularly in nutrient-scarce conditions. Experiments in Xenopus oocytes and flies indicate that Hodor is a pH-sensitive, zinc-gated chloride channel that mediates a previously unrecognized dietary preference for zinc. Hodor controls systemic growth from a subset of enterocytes-interstitial cells-by promoting food intake and insulin/IGF signalling. Although Hodor sustains gut luminal acidity and restrains microbial loads, its effect on systemic growth results from the modulation of Tor signalling and lysosomal homeostasis within interstitial cells. Hodor-like genes are insect-specific, and may represent targets for the control of disease vectors. Indeed, CRISPR-Cas9 genome editing revealed that the single hodor orthologue in Anopheles gambiae is an essential gene. Our findings highlight the need to consider the instructive contributions of metals-and, more generally, micronutrients-to energy homeostasis.


  
DNA clamp function of the monoubiquitinated Fanconi anaemia ID complex 期刊论文
NATURE, 2020, 580 (7802) : 278-+
作者:  Wu, Thomas D.;  39;Gorman, William E.
收藏  |  浏览/下载:8/0  |  提交时间:2020/07/03

The ID complex, involving the proteins FANCI and FANCD2, is required for the repair of DNA interstrand crosslinks (ICL) and related lesions(1). These proteins are mutated in Fanconi anaemia, a disease in which patients are predisposed to cancer. The Fanconi anaemia pathway of ICL repair is activated when a replication fork stalls at an ICL2  this triggers monoubiquitination of the ID complex, in which one ubiquitin molecule is conjugated to each of FANCI and FANCD2. Monoubiquitination of ID is essential for ICL repair by excision, translesion synthesis and homologous recombination  however, its function remains unknown(1,3). Here we report a cryo-electron microscopy structure of the monoubiquitinated human ID complex bound to DNA, and reveal that it forms a closed ring that encircles the DNA. By comparison with the structure of the non-ubiquitinated ID complex bound to ICL DNA-which we also report here-we show that monoubiquitination triggers a complete rearrangement of the open, trough-like ID structure through the ubiquitin of one protomer binding to the other protomer in a reciprocal fashion. These structures-together with biochemical data-indicate that the monoubiquitinated ID complex loses its preference for ICL and related branched DNA structures, and becomes a sliding DNA clamp that can coordinate the subsequent repair reactions. Our findings also reveal how monoubiquitination in general can induce an alternative protein structure with a new function.


Cryo-EM structures of the FANCI-FANCD2 complex bound to DNA reveal that monoubiquitination triggers structural changes that enable the complex to function as a sliding DNA clamp and coordinate the repair of DNA interstrand crosslinks.