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Mingui Fu

As seen in: Nature, The Journal of Biological Chemistry
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Articles by Mingui Fu

Author Correction: Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote TH17 differentiation | Nature Immunology

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By Desheng Hu, Sven Brenner, Jessica Zöller, Gitta A. Heinz, Daniel Nagel, Katharina U. Vogel, Nina Rehage, Renee Gloury, Nina M Martin, Maciej Lech, Arie Geerlof, Achim Weber, Hans-Joachim Anders Verified, Ingo Schmitz, Marc Schmidt-Supprian, Mingui Fu, Helmut Holtmann, Daniel Krappmann, Jürgen Ruland, Axel Kallies, Mathias Heikenwalder, Vigo Heissmeyer, Katharina M. Jeltsch, Sebastian C. Warth, Stephanie L. Edelmann, Claudia Lohs, Jenny E. Stehklein, Elisabeth Kremmer
| Nature Verified
Correction to: Nature Immunology https://doi.org/10.1038/ni.3008, published online 5 October 2014. In the version of this article initially published, due to a copy / paste error during figure preparation, in Fig. 7f, the WT plot was an inadvertent duplicate of the adjacent R510G,R579G plot. Due to the age of the article, the figure cannot be updated directly. The corrected Fig. 7f is available as Supplementary Information accompanying this amendment. This notice serves to correct the article.
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Lectin-based detection and expression profiling of native glycoRNAs - Scientific Reports

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By Yong Li, Yisong Qian, Xiang Li, Tianhua Lei, Hillary McGraw, Paula Monaghan-Nichols, Mingui Fu
| Nature Verified
Abstract Current methods for detecting glycoRNAs include metabolic labeling in living cells or animals and RNA-optimized periodate oxidation and aldehyde labeling (rPAL), each of which offers distinct advantages and limitations. Here, we report a relatively simple and rapid approach for detecting native glycoRNAs using direct lectin hybridization. This method involves several straightforward steps, including total RNA isolation, northern blotting, and lectin hybridization.
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Interaction between the PH and START domains of ceramide transfer protein competes with phosphatidylinositol 4-phosphate binding by the PH domain

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By Jennifer Prashek, Samuel Bouyain, Mingui Fu
| The Journal of Biological Chemistry Verified
De novo synthesis of the sphingolipid sphingomyelin requires non-vesicular transport of ceramide from the endoplasmic reticulum to the Golgi by the multidomain protein ceramide transfer protein (CERT). CERT's N-terminal pleckstrin homology (PH) domain targets it to the Golgi by binding to phosphatidylinositol 4-phosphate (PtdIns(4)P) in the Golgi membrane, whereas its C-terminal StAR-related lipid transfer domain (START) carries out ceramide transfer.
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