Structural and functional control of the eukaryotic mRNA decapping machinery

被引:80
作者
Arribas-Layton, Marcos [1 ]
Wu, Donghui [2 ]
Lykke-Andersen, Jens [1 ]
Song, Haiwei [2 ]
机构
[1] Univ Calif San Diego, Div Biol Sci, La Jolla, CA 92093 USA
[2] Inst Mol & Cell Biol, Lab Macromol Struct, Singapore 138673, Singapore
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS | 2013年 / 1829卷 / 6-7期
关键词
Decapping; Dcp2; Dcp1; Enhancer of decapping; mRNA decay; TRANSLATION INITIATION-FACTOR; DOMAIN-PEPTIDE COMPLEX; SM-LIKE PROTEINS; P-BODY FORMATION; CRYSTAL-STRUCTURE; SACCHAROMYCES-CEREVISIAE; BINDING-PROTEIN; LSM PROTEINS; HUMAN DCP2; DECAY;
D O I
10.1016/j.bbagrm.2012.12.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The regulation of mRNA degradation is critical for proper gene expression. Many major pathways for mRNA decay involve the removal of the 5' 7-methyl guanosine (m(7)G) cap in the cytoplasm to allow for 5'-to-3' exonucleolytic decay. The most well studied and conserved eukaryotic decapping enzyme is Dcp2, and its function is aided by co-factors and decapping enhancers. A subset of these factors can act to enhance the catalytic activity of Dcp2, while others might stimulate the remodeling of proteins bound to the mRNA substrate that may otherwise inhibit decapping. Structural studies have provided major insights into the mechanisms by which Dcp2 and decapping co-factors activate decapping. Additional mRNA decay factors can function by recruiting components of the decapping machinery to target mRNAs. mRNA decay factors, decapping factors, and mRNA substrates can be found in cytoplasmic foci named P bodies that are conserved in eukaryotes, though their function remains unknown. In addition to Dcp2, other decapping enzymes have been identified, which may serve to supplement the function of Dcp2 or act in independent decay or quality control pathways. This article is part of a Special Issue entitled: RNA Decay mechanisms. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:580 / 589
页数:10
相关论文
共 129 条
  • [1] Novel Sm-like proteins with long C-terminal tails and associated methyltransferases
    Albrecht, M
    Lengauer, T
    [J]. FEBS LETTERS, 2004, 569 (1-3) : 18 - 26
  • [2] Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability
    Anantharaman, V
    Aravind, L
    [J]. BMC GENOMICS, 2004, 5 (1)
  • [3] A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
    Andrei, MA
    Ingelfinger, D
    Heintzmann, R
    Achsel, T
    Rivera-Pomar, R
    Lührmann, R
    [J]. RNA, 2005, 11 (05) : 717 - 727
  • [4] Targeted mRNA degradation by deadenylation-independent decapping
    Badis, G
    Saveanu, C
    Fromont-Racine, M
    Jacquier, A
    [J]. MOLECULAR CELL, 2004, 15 (01) : 5 - 15
  • [5] EVH 1 domains: structure, function and interactions
    Ball, LJ
    Jarchau, T
    Oschkinat, H
    Walter, U
    [J]. FEBS LETTERS, 2002, 513 (01) : 45 - 52
  • [6] An essential component of the decapping enzyme required for normal rates of mRNA turnover
    Beelman, CA
    Stevens, A
    Caponigro, G
    LaGrandeur, TE
    Hatfield, L
    Fortner, DM
    Parker, R
    [J]. NATURE, 1996, 382 (6592) : 642 - 646
  • [7] Lsm proteins and RNA processing
    Beggs, JD
    [J]. BIOCHEMICAL SOCIETY TRANSACTIONS, 2005, 33 : 433 - 438
  • [8] MRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes
    Behm-Ansmant, Isabelle
    Rehwinkel, Jan
    Doerks, Tobias
    Stark, Alexander
    Bork, Peer
    Izaurralde, Elisa
    [J]. GENES & DEVELOPMENT, 2006, 20 (14) : 1885 - 1898
  • [9] Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition
    Beneken, J
    Tu, JC
    Xiao, B
    Nuriya, M
    Yuan, JP
    Worley, PF
    Leahy, DJ
    [J]. NEURON, 2000, 26 (01) : 143 - 154
  • [10] The MutT proteins or ''nudix'' hydrolases, a family of versatile, widely distributed, ''housecleaning'' enzymes
    Bessman, MJ
    Frick, DN
    OHandley, SF
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (41) : 25059 - 25062