Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation

Seminars in Cell & Developmental Biology - Tập 23 Số 5 - Trang 530-537 - 2012
Eric K. Fredrickson1, Richard G. Gardner1
1Department of Pharmacology, University of Washington, Seattle, WA 98195, USA

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Tài liệu tham khảo

Balch, 2008, Adapting proteostasis for disease intervention, Science, 319, 916, 10.1126/science.1141448

Wickner, 1999, Posttranslational quality control: folding, refolding, and degrading proteins, Science, 286, 1888, 10.1126/science.286.5446.1888

Akerfelt, 2010, Heat shock factors: integrators of cell stress, development and lifespan, Nat Rev Mol Cell Biol, 11, 545, 10.1038/nrm2938

Ron, 2007, Signal integration in the endoplasmic reticulum unfolded protein response, Nat Rev Mol Cell Biol, 8, 519, 10.1038/nrm2199

Voisine, 2010, Chaperone networks: tipping the balance in protein folding diseases, Neurobiol Dis, 40, 12, 10.1016/j.nbd.2010.05.007

Hartl, 2011, Molecular chaperones in protein folding and proteostasis, Nature, 475, 324, 10.1038/nature10317

de la Torre-Ruiz, 2010, How budding yeast sense and transduce the oxidative stress signal and the impact in cell growth and morphogenesis, Curr Protein Pept Sci, 11, 669, 10.2174/138920310794557628

Glickman, 2002, The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction, Physiol Rev, 82, 373, 10.1152/physrev.00027.2001

Ravid, 2008, Diversity of degradation signals in the ubiquitin-proteasome system, Nat Rev Mol Cell Biol, 9, 679, 10.1038/nrm2468

Petroski, 2005, Function and regulation of cullin-RING ubiquitin ligases, Nat Rev Mol Cell Biol, 6, 9, 10.1038/nrm1547

Bordallo, 1998, Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins, Mol Biol Cell, 9, 209, 10.1091/mbc.9.1.209

Hampton, 1996, Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein, Mol Biol Cell, 7, 2029, 10.1091/mbc.7.12.2029

Gardner, 2000, Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p, J Cell Biol, 151, 69, 10.1083/jcb.151.1.69

Deak, 2001, Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation, J Biol Chem, 276, 10663, 10.1074/jbc.M008608200

Fang, 2001, The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum, Proc Natl Acad Sci USA, 98, 14422, 10.1073/pnas.251401598

Kaneko, 2002, Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation, FEBS Lett, 532, 147, 10.1016/S0014-5793(02)03660-8

Lerner, 2007, The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD, Mol Biol Cell, 18, 1670, 10.1091/mbc.E06-03-0248

Nadav, 2003, A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1, Biochem Biophys Res Commun, 303, 91, 10.1016/S0006-291X(03)00279-1

Kikkert, 2004, Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum, J Biol Chem, 279, 3525, 10.1074/jbc.M307453200

Hampton, 1997, Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase, Proc Natl Acad Sci USA, 94, 12944, 10.1073/pnas.94.24.12944

Friedlander, 2000, A regulatory link between ER-associated protein degradation and the unfolded-protein response, Nat Cell Biol, 2, 379, 10.1038/35017001

Bays, 2001, Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation, Nat Cell Biol, 3, 24, 10.1038/35050524

Biederer, 1997, Role of Cue1p in ubiquitination and degradation at the ER surface, Science, 278, 1806, 10.1126/science.278.5344.1806

Chen, 2006, The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site, Proc Natl Acad Sci USA, 103, 341, 10.1073/pnas.0506618103

Lilley, 2005, Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane, Proc Natl Acad Sci USA, 102, 14296, 10.1073/pnas.0505014102

Mueller, 2006, SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER, J Cell Biol, 175, 261, 10.1083/jcb.200605196

Plemper, 1999, Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation, J Cell Sci, 112, 4123, 10.1242/jcs.112.22.4123

Gauss, 2006, The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment, EMBO J, 25, 1827, 10.1038/sj.emboj.7601088

Schulze, 2005, The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway, J Mol Biol, 354, 1021, 10.1016/j.jmb.2005.10.020

Okuda-Shimizu, 2007, Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp, Mol Cell, 28, 544, 10.1016/j.molcel.2007.09.012

Kim, 2009, Usa1 protein facilitates substrate ubiquitylation through two separate domains, PLoS One, 4, e7604, 10.1371/journal.pone.0007604

Horn, 2009, Usa1 functions as a scaffold of the HRD-ubiquitin ligase, Mol Cell, 36, 782, 10.1016/j.molcel.2009.10.015

Carroll, 2010, Usa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase, J Biol Chem, 285, 5146, 10.1074/jbc.M109.067876

Carvalho, 2006, Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins, Cell, 126, 361, 10.1016/j.cell.2006.05.043

Sato, 2009, Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase, Mol Cell, 34, 212, 10.1016/j.molcel.2009.03.010

Knop, 1996, a novel protein specifically required for endoplasmic reticulum degradation in yeast, EMBO J, 15, 753, 10.1002/j.1460-2075.1996.tb00411.x

Lilley, 2004, A membrane protein required for dislocation of misfolded proteins from the ER, Nature, 429, 834, 10.1038/nature02592

Ye, 2004, A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol, Nature, 429, 841, 10.1038/nature02656

Greenblatt, 2011, Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant alpha-1 antitrypsin from the endoplasmic reticulum, Nat Struct Mol Biol, 18, 1147, 10.1038/nsmb.2111

Plemper, 1997, Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation, Nature, 388, 891, 10.1038/42276

Rudiger, 1997, Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries, EMBO J, 16, 1501, 10.1093/emboj/16.7.1501

Szathmary, 2005, Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD, Mol Cell, 19, 765, 10.1016/j.molcel.2005.08.015

Kim, 2005, Yos9p detects and targets misfolded glycoproteins for ER-associated degradation, Mol Cell, 19, 753, 10.1016/j.molcel.2005.08.010

Bhamidipati, 2005, Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen, Mol Cell, 19, 741, 10.1016/j.molcel.2005.07.027

Buschhorn, 2004, A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins, FEBS Lett, 577, 422, 10.1016/j.febslet.2004.10.039

Christianson, 2008, OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD, Nat Cell Biol, 10, 272, 10.1038/ncb1689

Gauss, 2006, A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery, Nat Cell Biol, 8, 849, 10.1038/ncb1445

Denic, 2006, A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation, Cell, 126, 349, 10.1016/j.cell.2006.05.045

Hosokawa, 2009, Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans, J Biol Chem, 284, 17061, 10.1074/jbc.M809725200

Quan, 2008, Defining the glycan destruction signal for endoplasmic reticulum-associated degradation, Mol Cell, 32, 870, 10.1016/j.molcel.2008.11.017

Xie, 2009, Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system, Mol Biol Cell, 20, 3317, 10.1091/mbc.E09-03-0231

Kostova, 2005, Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation, J Cell Sci, 118, 1485, 10.1242/jcs.01740

Spear, 2005, Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation, J Cell Biol, 169, 73, 10.1083/jcb.200411136

Benitez, 2011, a control protein for misfolded glycosylated and non-glycosylated proteins in ERAD, FEBS Lett, 585, 3015, 10.1016/j.febslet.2011.08.021

Jaenicke, 2011, Yos9p assists in the degradation of certain non-glycosylated proteins from the endoplasmic reticulum, Mol Biol Cell, 10.1091/mbc.E10-10-0832

Swanson, 2001, A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation, Genes Dev, 15, 2660, 10.1101/gad.933301

Huyer, 2004, Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein, J Biol Chem, 279, 38369, 10.1074/jbc.M402468200

Kreft, 2006, Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI), J Biol Chem, 281, 4646, 10.1074/jbc.M512215200

Zavacki, 2009, The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase, Mol Cell Biol, 29, 5339, 10.1128/MCB.01498-08

Ravid, 2006, Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways, EMBO J, 25, 533, 10.1038/sj.emboj.7600946

Liu, 2010, Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates, J Biol Chem, 285, 10265, 10.1074/jbc.M110.110551

Johnson, 1998, Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway, Cell, 94, 217, 10.1016/S0092-8674(00)81421-X

Metzger, 2008, Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery, J Biol Chem, 283, 32302, 10.1074/jbc.M806424200

Gilon, 1998, Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae, EMBO J, 17, 2759, 10.1093/emboj/17.10.2759

Gilon, 2000, Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair, Mol Cell Biol, 20, 7214, 10.1128/MCB.20.19.7214-7219.2000

Reggiori, 2002, A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies, Nat Cell Biol, 4, 117, 10.1038/ncb743

Hettema, 2004, Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins, EMBO J, 23, 1279, 10.1038/sj.emboj.7600137

Pizzirusso, 2004, Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast, Mol Biol Cell, 15, 2401, 10.1091/mbc.E03-10-0727

Kaganovich, 2008, Misfolded proteins partition between two distinct quality control compartments, Nature, 454, 1088, 10.1038/nature07195

Jiang, 2001, CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation, J Biol Chem, 276, 42938, 10.1074/jbc.M101968200

Ballinger, 1999, Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions, Mol Cell Biol, 19, 4535, 10.1128/MCB.19.6.4535

Connell, 2001, The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins, Nat Cell Biol, 3, 93, 10.1038/35050618

Murata, 2001, CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein, EMBO Rep, 2, 1133, 10.1093/embo-reports/kve246

Stankiewicz, 2010, CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates, FEBS J, 277, 3353, 10.1111/j.1742-4658.2010.07737.x

Rosser, 2007, Chaperone functions of the E3 ubiquitin ligase CHIP, J Biol Chem, 282, 22267, 10.1074/jbc.M700513200

Takayama, 1999, An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators, J Biol Chem, 274, 781, 10.1074/jbc.274.2.781

Dai, 2005, Regulation of the cytoplasmic quality control protein degradation pathway by BAG2, J Biol Chem, 280, 38673, 10.1074/jbc.M507986200

Kalia, 2011, Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5), PLoS One, 6, e14695, 10.1371/journal.pone.0014695

Luders, 2000, The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome, J Biol Chem, 275, 4613, 10.1074/jbc.275.7.4613

Gamerdinger, 2009, Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3, EMBO J, 28, 889, 10.1038/emboj.2009.29

Alberti, 2004, The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator, Mol Biol Cell, 15, 4003, 10.1091/mbc.E04-04-0293

Prasad, 2010, A nucleus-based quality control mechanism for cytosolic proteins, Mol Biol Cell, 21, 2117, 10.1091/mbc.E10-02-0111

Nillegoda, 2010, Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins, Mol Biol Cell, 21, 2102, 10.1091/mbc.E10-02-0098

Heck, 2010, Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1, Proc Natl Acad Sci USA, 107, 1106, 10.1073/pnas.0910591107

Eisele, 2008, Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1, FEBS Lett, 582, 4143, 10.1016/j.febslet.2008.11.015

Varshavsky, 2011, The N-end rule pathway and regulation by proteolysis, Protein Sci, 20, 1298, 10.1002/pro.666

Sultana, 2011, UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition, Exp Cell Res, 318, 53, 10.1016/j.yexcr.2011.09.010

Park, 2007, The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system, Mol Biol Cell, 18, 153, 10.1091/mbc.E06-04-0338

Hwang, 2010, N-terminal acetylation of cellular proteins creates specific degradation signals, Science, 327, 973, 10.1126/science.1183147

Fang, 2011, Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins, Nat Cell Biol, 13, 1344, 10.1038/ncb2343

Leggett, 2002, Multiple associated proteins regulate proteasome structure and function, Mol Cell, 10, 495, 10.1016/S1097-2765(02)00638-X

Aviram, 2010, The ubiquitin ligase Hul5 promotes proteasomal processivity, Mol Cell Biol, 30, 985, 10.1128/MCB.00909-09

Akimitsu, 2008, Messenger RNA surveillance systems monitoring proper translation termination, J Biochem, 143, 1, 10.1093/jb/mvm204

Dimitrova, 2009, Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome, J Biol Chem, 284, 10343, 10.1074/jbc.M808840200

Wilson, 2007, A genomic screen in yeast reveals novel aspects of nonstop mRNA metabolism, Genetics, 177, 773, 10.1534/genetics.107.073205

Braun, 2007, Identification of Rkr1, a nuclear RING domain protein with functional connections to chromatin modification in Saccharomyces cerevisiae, Mol Cell Biol, 27, 2800, 10.1128/MCB.01947-06

Bengtson, 2010, Role of a ribosome-associated E3 ubiquitin ligase in protein quality control, Nature, 467, 470, 10.1038/nature09371

Dasgupta, 2004, Sir antagonist 1 (San1) is a ubiquitin ligase, J Biol Chem, 279, 26830, 10.1074/jbc.M400894200

Gardner, 2005, Degradation-mediated protein quality control in the nucleus, Cell, 120, 803, 10.1016/j.cell.2005.01.016

Evans, 1998, The yeast protein complex containing cdc68 and pob3 mediates core-promoter repression through the cdc68 N-terminal domain, Genetics, 150, 1393, 10.1093/genetics/150.4.1393

Estruch, 2009, A genetic screen in Saccharomyces cerevisiae identifies new genes that interact with mex67-5, a temperature-sensitive allele of the gene encoding the mRNA export receptor, Mol Genet Genomics, 281, 125, 10.1007/s00438-008-0402-x

Lewis, 2009, Inefficient quality control of thermosensitive proteins on the plasma membrane, PLoS One, 4, e5038, 10.1371/journal.pone.0005038

Matsuo, 2011, Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast, J Biol Chem, 10.1074/jbc.M110.169953

Rosenbaum, 2011, Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates, Mol Cell, 41, 93, 10.1016/j.molcel.2010.12.004

Fredrickson, 2011, Exposed hydrophobicity is a key determinant of nuclear quality control degradation, Mol Biol Cell, 22, 2384, 10.1091/mbc.E11-03-0256

Deng, 2006, Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase, Nature, 443, 827, 10.1038/nature05170

Furth, 2011, Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope, Mol Biol Cell, 10.1091/mbc.E11-05-0463

Mullen, 2008, Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates, J Biol Chem, 283, 19912, 10.1074/jbc.M802690200

Xie, 2007, The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation, J Biol Chem, 282, 34176, 10.1074/jbc.M706025200

Wang, 2009, Quality control of a transcriptional regulator by SUMO-targeted degradation, Mol Cell Biol, 29, 1694, 10.1128/MCB.01470-08

Ward, 1994, Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins, J Biol Chem, 269, 25710, 10.1016/S0021-9258(18)47306-1

Ward, 1995, Degradation of CFTR by the ubiquitin-proteasome pathway, Cell, 83, 121, 10.1016/0092-8674(95)90240-6

Iwata, 2009, Intra-nuclear degradation of polyglutamine aggregates by the ubiquitin proteasome system, J Biol Chem, 284, 9796, 10.1074/jbc.M809739200

Janer, 2006, PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins, J Cell Biol, 174, 65, 10.1083/jcb.200511045

Fu, 2005, Nuclear aggresomes form by fusion of PML-associated aggregates, Mol Biol Cell, 16, 4905, 10.1091/mbc.E05-01-0019

Kaser, 2000, Protein degradation in mitochondria, Semin Cell Dev Biol, 11, 181, 10.1006/scdb.2000.0166

Kitada, 1998, Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism, Nature, 392, 605, 10.1038/33416

Morett, 1999, A novel transactivation domain in parkin, Trends Biochem Sci, 24, 229, 10.1016/S0968-0004(99)01381-X

Shimura, 2000, Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase, Nat Genet, 25, 302, 10.1038/77060

Zhang, 2000, Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1, Proc Natl Acad Sci USA, 97, 13354, 10.1073/pnas.240347797

Imai, 2002, CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity, Mol Cell, 10, 55, 10.1016/S1097-2765(02)00583-X

Tanaka, 2004, Ubiquitin, proteasome and parkin, Biochim Biophys Acta, 1695, 235, 10.1016/j.bbamcr.2004.09.026

Yonashiro, 2006, A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics, EMBO J, 25, 3618, 10.1038/sj.emboj.7601249

Yonashiro, 2009, Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation, Mol Biol Cell, 20, 4524, 10.1091/mbc.E09-02-0112