title: Mechanisms of endonuclease-mediated mRNA decay.
abstract: Endonuclease cleavage was one of the first identified mechanisms of mRNA decay but until recently it was thought to play a minor role to the better-known processes of deadenylation, decapping, and exonuclease-catalyzed decay. Most of the early examples of endonuclease decay came from studies of a particular mRNA whose turnover changed in response to hormone, cytokine, developmental, or nutritional stimuli. Only a few of these examples of endonuclease-mediated mRNA decay progressed to the point where the enzyme responsible for the initiating event was identified and studied in detail. The discovery of microRNAs and RISC-catalyzed endonuclease cleavage followed by the identification of PIN (pilT N-terminal) domains that impart endonuclease activity to a number of the proteins involved in mRNA decay has led to a resurgence of interest in endonuclease-mediated mRNA decay. PIN domains show no substrate selectivity and their involvement in a number of decay pathways highlights a recurring theme that the context in which an endonuclease function is a primary factor in determining whether any given mRNA will be targeted for decay by this or the default exonuclease-mediated decay processes.
authors.affiliation: Center for RNA Biology and Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, OH, USA. schoenberg.3@osu.edu
authors.forename: Daniel R
authors.initials: DR
authors.lastname: Schoenberg
mesh_terms: D000818:Animals; D001053:Apolipoproteins / Q000235:genetics; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D050760:Cyclin-Dependent Kinase Inhibitor p27 / Q000235:genetics; D004265:DNA Helicases; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase / Q000235:genetics / Q000378:metabolism; D004720:Endonucleases / Q000235:genetics / Q000378:metabolism*; D004722:Endoribonucleases / Q000235:genetics / Q000378:metabolism; D005260:Female; D018398:Homeodomain Proteins / Q000235:genetics; D006801:Humans; D007335:Insulin-Like Growth Factor II / Q000235:genetics; D016209:Interleukin-8 / Q000235:genetics; D008079:Lipoproteins, VLDL / Q000235:genetics; D008297:Male; D051379:Mice; D008954:Models, Biological; D000075223:Poly-ADP-Ribose Binding Proteins; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D020365:RNA Helicases; D000067776:RNA Recognition Motif Proteins; D020871:RNA Stability / Q000235:genetics / Q000502:physiology*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D011990:Receptors, Transferrin / Q000235:genetics; D012260:Ribonucleases / Q000235:genetics / Q000378:metabolism; D019098:Telomerase / Q000235:genetics / Q000378:metabolism; D055542:alpha-Globins / Q000235:genetics
chemical_list: D001053:Apolipoproteins; D002352:Carrier Proteins; D018398:Homeodomain Proteins; D016209:Interleukin-8; D008079:Lipoproteins, VLDL; D000075223:Poly-ADP-Ribose Binding Proteins; D000067776:RNA Recognition Motif Proteins; D012333:RNA, Messenger; D011990:Receptors, Transferrin; D055542:alpha-Globins; C027610:apolipoprotein VLDL II; D050760:Cyclin-Dependent Kinase Inhibitor p27; D007335:Insulin-Like Growth Factor II; C510185:Ern1 protein, mouse; D017346:Protein Serine-Threonine Kinases; D019098:Telomerase; D004720:Endonucleases; D004722:Endoribonucleases; D012260:Ribonucleases; C512261:SMG6 protein, human; C541320:Zc3h12a protein, mouse; C116181:polysomal RNase 1; D004265:DNA Helicases; C492055:G3bp1 protein, mouse; D020365:RNA Helicases; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase