title: Protein segregase meddles in remodeling of mRNA-protein complexes.
abstract: Remodeling of RNA-protein complexes (mRNPs) plays a critical role in mRNA biogenesis and metabolism. However, relatively little is known about the underlying mechanism and regulation of the mRNP remodeling. In this issue of Genes & Development, Zhou and colleagues (pp. 1046-1058) report that a protein remodeling machine, the p97-UBXD8 complex, disassembles mRNPs containing the AU-rich elements (AREs) bound by HuR proteins in a nondegradative, ubiquitin signaling-dependent manner, revealing a novel mechanism to regulate mRNA turnover.
authors: Department of Biochemistry and Molecular Biology, The University of Texas Medical School at Houston, Houston, Texas 77030, USA.
authors: Chyi-Ying A
authors: CY
authors: Chen
authors: Ann-Bin
authors: AB
authors: Shyu
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D051959:ELAV Proteins / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D020871:RNA Stability; D012333:RNA, Messenger / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism*
chemical_list: D001798:Blood Proteins; D051959:ELAV Proteins; C468782:FAF2 protein, human; D008565:Membrane Proteins; D009687:Nuclear Proteins; D012333:RNA, Messenger; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein; D000251:Adenosine Triphosphatases; C404942:p97 ATPase
keywords: HuR; mRNA stability; ubiquitin
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