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Schmider, Angela

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Schmider

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Angela

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Schmider, Angela

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2015 - 20162

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Author's Publications: search.filters.isAuthorOfPublication.5dfaae30-f021-4344-970f-bb3d26e86b77

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    Diabetes regulates fructose absorption through thioredoxin-interacting protein
    (eLife Sciences Publications, Ltd, 2016) Dotimas, James R; Lee, Austin W; Schmider, Angela; Carroll, Shannon; Shah, Anu; Bilen, Julide; Elliott, Kayla R; Myers, Ronald B; Soberman, Roy; Yoshioka, Jun; Lee, Richard
    Metabolic studies suggest that the absorptive capacity of the small intestine for fructose is limited, though the molecular mechanisms controlling this process remain unknown. Here we demonstrate that thioredoxin-interacting protein (Txnip), which regulates glucose homeostasis in mammals, binds to fructose transporters and promotes fructose absorption by the small intestine. Deletion of Txnip in mice reduced fructose transport into the peripheral bloodstream and liver, as well as the severity of adverse metabolic outcomes resulting from long-term fructose consumption. We also demonstrate that fructose consumption induces expression of Txnip in the small intestine. Diabetic mice had increased expression of Txnip in the small intestine as well as enhanced fructose uptake and transport into the hepatic portal circulation. The deletion of Txnip in mice abolished the diabetes-induced increase in fructose absorption. Our results indicate that Txnip is a critical regulator of fructose metabolism and suggest that a diabetic state can promote fructose uptake. DOI: http://dx.doi.org/10.7554/eLife.18313.001
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    Coordinated regulation of bidirectional COPI transport at the Golgi by cdc42
    (2015) Park, Seung-Yeol; Yang, Jia-Shu; Schmider, Angela; Soberman, Roy; Hsu, Victor
    The Golgi complex plays a central role in the intracellular sorting of secretory proteins 1,2. Anterograde transport through the Golgi has been explained by the movement of Golgi cisternae, known as cisternal maturation 3–5. Because this explanation is now appreciated to be incomplete 6, interest has developed in understanding tubules that connect the Golgi cisternae 7–9. Here, we find that the Coat Protein I (COPI) complex sorts anterograde cargoes into these tubules. Moreover, the small GTPase cdc42 regulates bidirectional Golgi transport by targeting the dual functions of COPI in cargo sorting and carrier formation. Cdc42 also directly imparts membrane curvature in promoting COPI tubule formation. Our findings further reveal that COPI tubular transport complements cisternal maturation in explaining how anterograde Golgi transport is achieved, and that bidirectional COPI transport is modulated by environmental cues through cdc42.