Hul5 ubiquitin ligase

References

• McClellan AJ, Tam S, Kaganovich D, Frydman J. Protein quality control: chaperones culling corrupt conformations. Nat Cell Biol 2005; 7:736 - 41; http://dx.doi.org/10.1038/ncb0805-736; PMID: 16056264
   PubMed Web of Science ®Google Scholar
• Wickner S, Maurizi MR, Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 1999; 286:1888 - 93; http://dx.doi.org/10.1126/science.286.5446.1888; PMID: 10583944
   PubMed Web of Science ®Google Scholar
• Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science 2008; 319:916 - 9; http://dx.doi.org/10.1126/science.1141448; PMID: 18276881
   PubMed Web of Science ®Google Scholar
• Vembar SS, Brodsky JL. One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 2008; 9:944 - 57; http://dx.doi.org/10.1038/nrm2546; PMID: 19002207
   PubMed Web of Science ®Google Scholar
• Ravid T, Hochstrasser M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat Rev Mol Cell Biol 2008; 9:679 - 90; http://dx.doi.org/10.1038/nrm2468; PMID: 18698327
   PubMed Web of Science ®Google Scholar
• Rosenbaum JC, Gardner RG. How a disordered ubiquitin ligase maintains order in nuclear protein homeostasis. Nucleus 2011; 2; http://dx.doi.org/10.4161/nucl.2.4.16118; PMID: 21941105
   PubMedGoogle Scholar
• Connell P, Ballinger CA, Jiang J, Wu Y, Thompson LJ, Höhfeld J, et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol 2001; 3:93 - 6; http://dx.doi.org/10.1038/35050618; PMID: 11146632
   PubMed Web of Science ®Google Scholar
• Murata S, Minami Y, Minami M, Chiba T, Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep 2001; 2:1133 - 8; http://dx.doi.org/10.1093/embo-reports/kve246; PMID: 11743028
   PubMed Web of Science ®Google Scholar
• Heck JW, Cheung SK, Hampton RY. Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc Natl Acad Sci U S A 2010; 107:1106 - 11; http://dx.doi.org/10.1073/pnas.0910591107; PMID: 20080635
   PubMed Web of Science ®Google Scholar
• Prasad R, Kawaguchi S, Ng DT. A nucleus-based quality control mechanism for cytosolic proteins. Mol Biol Cell 2010; 21:2117 - 27; http://dx.doi.org/10.1091/mbc.E10-02-0111; PMID: 20462951
   PubMed Web of Science ®Google Scholar
• Sultana R, Theodoraki MA, Caplan AJ. UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition. Exp Cell Res 2012; 318:53 - 60; http://dx.doi.org/10.1016/j.yexcr.2011.09.010; PMID: 21983172
   PubMed Web of Science ®Google Scholar
• Nillegoda NB, Theodoraki MA, Mandal AK, Mayo KJ, Ren HY, Sultana R, et al. Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol Biol Cell 2010; 21:2102 - 16; http://dx.doi.org/10.1091/mbc.E10-02-0098; PMID: 20462952
   PubMed Web of Science ®Google Scholar
• Bengtson MH, Joazeiro CA. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 2010; 467:470 - 3; http://dx.doi.org/10.1038/nature09371; PMID: 20835226
   PubMed Web of Science ®Google Scholar
• Fang NN, Ng AH, Measday V, Mayor T. Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat Cell Biol 2011; 13:1344 - 52; http://dx.doi.org/10.1038/ncb2343; PMID: 21983566
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 2001; 106:171 - 82; http://dx.doi.org/10.1016/S0092-8674(01)00427-5; PMID: 11511345
   PubMed Web of Science ®Google Scholar
• Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, et al. System-wide changes to SUMO modifications in response to heat shock. Sci Signal 2009; 2:ra24; http://dx.doi.org/10.1126/scisignal.2000282; PMID: 19471022
   PubMed Web of Science ®Google Scholar
• Miller MJ, Barrett-Wilt GA, Hua Z, Vierstra RD. Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis. Proc Natl Acad Sci U S A 2010; 107:16512 - 7; http://dx.doi.org/10.1073/pnas.1004181107; PMID: 20813957
   PubMed Web of Science ®Google Scholar
• Crosas B, Hanna J, Kirkpatrick DS, Zhang DP, Tone Y, Hathaway NA, et al. Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 2006; 127:1401 - 13; http://dx.doi.org/10.1016/j.cell.2006.09.051; PMID: 17190603
   PubMed Web of Science ®Google Scholar
• Aviram S, Kornitzer D. The ubiquitin ligase Hul5 promotes proteasomal processivity. Mol Cell Biol 2010; 30:985 - 94; http://dx.doi.org/10.1128/MCB.00909-09; PMID: 20008553
   PubMed Web of Science ®Google Scholar
• Seufert W, Jentsch S. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 1990; 9:543 - 50; PMID: 2154373
   PubMed Web of Science ®Google Scholar
• Medicherla B, Goldberg AL. Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins. J Cell Biol 2008; 182:663 - 73; http://dx.doi.org/10.1083/jcb.200803022; PMID: 18725537
   PubMed Web of Science ®Google Scholar
• McClellan AJ, Scott MD, Frydman J. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 2005; 121:739 - 48; http://dx.doi.org/10.1016/j.cell.2005.03.024; PMID: 15935760
   PubMed Web of Science ®Google Scholar
• Park SH, Bolender N, Eisele F, Kostova Z, Takeuchi J, Coffino P, et al. The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. Mol Biol Cell 2007; 18:153 - 65; http://dx.doi.org/10.1091/mbc.E06-04-0338; PMID: 17065559
   PubMed Web of Science ®Google Scholar
• Han S, Liu Y, Chang A. Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1. J Biol Chem 2007; 282:26140 - 9; http://dx.doi.org/10.1074/jbc.M701969200; PMID: 17631501
   PubMed Web of Science ®Google Scholar
• Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS, et al. Global analysis of protein localization in budding yeast. Nature 2003; 425:686 - 91; http://dx.doi.org/10.1038/nature02026; PMID: 14562095
   PubMed Web of Science ®Google Scholar
• Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008; 454:1088 - 95; http://dx.doi.org/10.1038/nature07195; PMID: 18756251
   PubMed Web of Science ®Google Scholar
• Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, et al. Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 2011; 41:93 - 106; http://dx.doi.org/10.1016/j.molcel.2010.12.004; PMID: 21211726
   PubMed Web of Science ®Google Scholar
• Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999; 96:635 - 44; http://dx.doi.org/10.1016/S0092-8674(00)80574-7; PMID: 10089879
   PubMed Web of Science ®Google Scholar
• Torres EM, Dephoure N, Panneerselvam A, Tucker CM, Whittaker CA, Gygi SP, et al. Identification of aneuploidy-tolerating mutations. Cell 2010; 143:71 - 83; http://dx.doi.org/10.1016/j.cell.2010.08.038; PMID: 20850176
   PubMed Web of Science ®Google Scholar
• Lee BH, Lee MJ, Park S, Oh DC, Elsasser S, Chen PC, et al. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 2010; 467:179 - 84; http://dx.doi.org/10.1038/nature09299; PMID: 20829789
   PubMed Web of Science ®Google Scholar
• Chernova TA, Romanyuk AV, Karpova TS, Shanks JR, Ali M, Moffatt N, et al. Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Mol Cell 2011; 43:242 - 52; http://dx.doi.org/10.1016/j.molcel.2011.07.001; PMID: 21777813
   PubMed Web of Science ®Google Scholar
• Pasaje CF, Kim JH, Park BL, Park JS, Uh ST, Kim MK, et al. UBE3C genetic variations as potent markers of nasal polyps in Korean asthma patients. J Hum Genet 2011; 56:797 - 800; http://dx.doi.org/10.1038/jhg.2011.104; PMID: 21881582
   PubMed Web of Science ®Google Scholar
• Yu Y, Hayward GS. The ubiquitin E3 ligase RAUL negatively regulates type i interferon through ubiquitination of the transcription factors IRF7 and IRF3. Immunity 2010; 33:863 - 77; http://dx.doi.org/10.1016/j.immuni.2010.11.027; PMID: 21167755
   PubMed Web of Science ®Google Scholar