Search

Your search keyword '"Eric Cockman"' showing total 2 results
Start Over Author "Eric Cockman"
2 results on '"Eric Cockman"'

1. TOP mRNPs: Molecular Mechanisms and Principles of Regulation

Author

Eric Cockman, Paul Anderson, and Pavel Ivanov

Subjects
5’ Terminal Oligopyrimidine, RNA binding proteins, LARP1, translation regulation, RNA, Microbiology, QR1-502
Abstract

The cellular response to changes in the surrounding environment and to stress requires the coregulation of gene networks aiming to conserve energy and resources. This is often achieved by downregulating protein synthesis. The 5’ Terminal OligoPyrimidine (5’ TOP) motif-containing mRNAs, which encode proteins that are essential for protein synthesis, are the primary targets of translational control under stress. The TOP motif is a cis-regulatory RNA element that begins directly after the m7G cap structure and contains the hallmark invariant 5’-cytidine followed by an uninterrupted tract of 4–15 pyrimidines. Regulation of translation via the TOP motif coordinates global protein synthesis with simultaneous co-expression of the protein components required for ribosome biogenesis. In this review, we discuss architecture of TOP mRNA-containing ribonucleoprotein complexes, the principles of their assembly, and the modes of regulation of TOP mRNA translation.

Published
2020
Full Text
View/download PDF

2. IL-17-receptor-associated adaptor Act1 directly stabilizes mRNAs to mediate IL-17 inflammatory signaling

Author

Jodi L. Bubenik, Xing Chen, Donny D. Licatalosi, Kommireddy Vasu, Hui Yang, Tomasz Herjan, Xiao Li, Caini Liu, Xiaoxia Li, Katarzyna Bulek, Wen Qian, Suidong Ouyang, Jun Qin, Kewal Asosingh, Paul L. Fox, Lingzi Hong, Eric Cockman, Thomas A. Hamilton, Junjie Zhao, Mark A. Aronica, Donna M. Driscoll, and Hao Zhou

Subjects
0301 basic medicine, Untranslated region, Chemokine, RNA Stability, Immunology, Mice, 03 medical and health sciences, 0302 clinical medicine, P-bodies, Animals, Immunology and Allergy, RNA, Messenger, Adaptor Proteins, Signal Transducing, Inflammation, Messenger RNA, Receptors, Interleukin-17, biology, Chemistry, Interleukin-17, Signal transducing adaptor protein, RNA, Translation (biology), MRNA stabilization, Cell biology, Mice, Inbred C57BL, 030104 developmental biology, Gene Expression Regulation, biology.protein, Signal Transduction, 030215 immunology
Abstract

Mechanisms that degrade inflammatory mRNAs are well known; however, stabilizing mechanisms are poorly understood. Here, we show that Act1, an interleukin-17 (IL-17)-receptor-complex adaptor, binds and stabilizes mRNAs encoding key inflammatory proteins. The Act1 SEFIR domain binds a stem-loop structure, the SEFIR-binding element (SBE), in the 3' untranslated region (UTR) of Cxcl1 mRNA, encoding an inflammatory chemokine. mRNA-bound Act1 directs formation of three compartmentally distinct RNA-protein complexes (RNPs) that regulate three disparate events in inflammatory-mRNA metabolism: preventing mRNA decay in the nucleus, inhibiting mRNA decapping in P bodies and promoting translation. SBE RNA aptamers decreased IL-17-mediated mRNA stabilization in vitro, IL-17-induced skin inflammation and airway inflammation in a mouse asthma model, thus providing a therapeutic strategy for autoimmune diseases. These results reveal a network in which Act1 assembles RNPs on the 3' UTRs of select mRNAs and consequently controls receptor-mediated mRNA stabilization and translation during inflammation.

Published
2018
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results