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Volumn 55, Issue 2, 2014, Pages 227-237

Cytosolic Quality Control of Mislocalized Proteins Requires RNF126 Recruitment to Bag6

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; LYSINE; PROTEASOME; PROTEIN BAG6; PROTEIN RNF126; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84904567733     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.05.025     Document Type: Article
Times cited : (145)

References (51)
  • 2
    • 0025013749 scopus 로고
    • Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism
    • Arnold A., Horst S.A., Gardella T.J., Baba H., Levine M.A., Kronenberg H.M. Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism. J.Clin. Invest. 1990, 86:1084-1087.
    • (1990) J.Clin. Invest. , vol.86 , pp. 1084-1087
    • Arnold, A.1    Horst, S.A.2    Gardella, T.J.3    Baba, H.4    Levine, M.A.5    Kronenberg, H.M.6
  • 3
    • 54249087710 scopus 로고    scopus 로고
    • Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation
    • Ashok A., Hegde R.S. Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation. Mol. Biol. Cell 2008, 19:3463-3476.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3463-3476
    • Ashok, A.1    Hegde, R.S.2
  • 4
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.Y., Patterson C. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 1999, 19:4535-4545.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 5
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson M.H., Joazeiro C.A. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 2010, 467:470-473.
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 6
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
    • Buchberger A., Bukau B., Sommer T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell 2010, 40:238-252.
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 7
    • 82955207151 scopus 로고    scopus 로고
    • BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum
    • Claessen J.H., Ploegh H.L. BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum. PLoS ONE 2011, 6:e28542.
    • (2011) PLoS ONE , vol.6
    • Claessen, J.H.1    Ploegh, H.L.2
  • 9
    • 84890085638 scopus 로고    scopus 로고
    • Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging
    • Cuanalo-Contreras K., Mukherjee A., Soto C. Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging. Int. J. Cell Biol. 2013, 2013:638083.
    • (2013) Int. J. Cell Biol. , vol.2013 , pp. 638083
    • Cuanalo-Contreras, K.1    Mukherjee, A.2    Soto, C.3
  • 10
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma N.P., Lindsten K., Glas R., Jellne M., Masucci M.G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 2000, 18:538-543.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 11
    • 84872559920 scopus 로고    scopus 로고
    • Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase
    • Delker R.K., Zhou Y., Strikoudis A., Stebbins C.E., Papavasiliou F.N. Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase. Proc. Natl. Acad. Sci. USA 2013, 110:1029-1034.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1029-1034
    • Delker, R.K.1    Zhou, Y.2    Strikoudis, A.3    Stebbins, C.E.4    Papavasiliou, F.N.5
  • 12
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: protein disaggregating machines
    • Doyle S.M., Wickner S. Hsp104 and ClpB: protein disaggregating machines. Trends Biochem. Sci. 2009, 34:40-48.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 13
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi B., Stewart R.S., Adles C., Stewart L.R., Quaglio E., Biasini E., Fioriti L., Chiesa R., Harris D.A. Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J.Biol. Chem. 2003, 278:21732-21743.
    • (2003) J.Biol. Chem. , vol.278 , pp. 21732-21743
    • Drisaldi, B.1    Stewart, R.S.2    Adles, C.3    Stewart, L.R.4    Quaglio, E.5    Biasini, E.6    Fioriti, L.7    Chiesa, R.8    Harris, D.A.9
  • 14
    • 57049182407 scopus 로고    scopus 로고
    • Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
    • Eisele F., Wolf D.H. Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1. FEBS Lett. 2008, 582:4143-4146.
    • (2008) FEBS Lett. , vol.582 , pp. 4143-4146
    • Eisele, F.1    Wolf, D.H.2
  • 15
    • 70349778618 scopus 로고    scopus 로고
    • The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
    • Ernst R., Mueller B., Ploegh H.L., Schlieker C. The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol. Cell 2009, 36:28-38.
    • (2009) Mol. Cell , vol.36 , pp. 28-38
    • Ernst, R.1    Mueller, B.2    Ploegh, H.L.3    Schlieker, C.4
  • 16
    • 84863653991 scopus 로고    scopus 로고
    • Hul5 ubiquitin ligase: good riddance to bad proteins
    • Fang N.N., Mayor T. Hul5 ubiquitin ligase: good riddance to bad proteins. Prion 2012, 6:240-244.
    • (2012) Prion , vol.6 , pp. 240-244
    • Fang, N.N.1    Mayor, T.2
  • 17
    • 0028149893 scopus 로고
    • Common and divergent peptide binding specificities of hsp70 molecular chaperones
    • Fourie A.M., Sambrook J.F., Gething M.J. Common and divergent peptide binding specificities of hsp70 molecular chaperones. J.Biol. Chem. 1994, 269:30470-30478.
    • (1994) J.Biol. Chem. , vol.269 , pp. 30470-30478
    • Fourie, A.M.1    Sambrook, J.F.2    Gething, M.J.3
  • 18
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • Gardner R.G., Nelson Z.W., Gottschling D.E. Degradation-mediated protein quality control in the nucleus. Cell 2005, 120:803-815.
    • (2005) Cell , vol.120 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 19
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck J.W., Cheung S.K., Hampton R.Y. Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl. Acad. Sci. USA 2010, 107:1106-1111.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 21
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation are coupled for elimination of mislocalized proteins
    • Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E., Hegde R.S. Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature 2011, 475:394-397.
    • (2011) Nature , vol.475 , pp. 394-397
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 22
    • 84878223129 scopus 로고    scopus 로고
    • Permanent neonatal diabetes due to a novel insulin signal peptide mutation
    • Hussain S., Mohd Ali J., Jalaludin M.Y., Harun F. Permanent neonatal diabetes due to a novel insulin signal peptide mutation. Pediatr. Diabetes 2013, 14:299-303.
    • (2013) Pediatr. Diabetes , vol.14 , pp. 299-303
    • Hussain, S.1    Mohd Ali, J.2    Jalaludin, M.Y.3    Harun, F.4
  • 23
    • 84874506372 scopus 로고    scopus 로고
    • Hsp90: structure and function
    • Jackson S.E. Hsp90: structure and function. Top. Curr. Chem. 2013, 328:155-240.
    • (2013) Top. Curr. Chem. , vol.328 , pp. 155-240
    • Jackson, S.E.1
  • 25
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang S.W., Rane N.S., Kim S.J., Garrison J.L., Taunton J., Hegde R.S. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 2006, 127:999-1013.
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 26
    • 84878191743 scopus 로고    scopus 로고
    • BAG6/BAT3: emerging roles in quality control for nascent polypeptides
    • Kawahara H., Minami R., Yokota N. BAG6/BAT3: emerging roles in quality control for nascent polypeptides. J.Biochem. 2013, 153:147-160.
    • (2013) J.Biochem. , vol.153 , pp. 147-160
    • Kawahara, H.1    Minami, R.2    Yokota, N.3
  • 27
    • 77952851112 scopus 로고    scopus 로고
    • Chaperone-assisteddegradation: multiple paths to destruction
    • Kettern N., Dreiseidler M., Tawo R., Höhfeld J. Chaperone-assisteddegradation: multiple paths to destruction. Biol. Chem. 2010, 391:481-489.
    • (2010) Biol. Chem. , vol.391 , pp. 481-489
    • Kettern, N.1    Dreiseidler, M.2    Tawo, R.3    Höhfeld, J.4
  • 28
    • 0036481454 scopus 로고    scopus 로고
    • Signal sequences control gating of the protein translocation channel in a substrate-specific manner
    • Kim S.J., Mitra D., Salerno J.R., Hegde R.S. Signal sequences control gating of the protein translocation channel in a substrate-specific manner. Dev. Cell 2002, 2:207-217.
    • (2002) Dev. Cell , vol.2 , pp. 207-217
    • Kim, S.J.1    Mitra, D.2    Salerno, J.R.3    Hegde, R.S.4
  • 30
    • 11144255136 scopus 로고    scopus 로고
    • The efficiency of protein compartmentalization into the secretory pathway
    • Levine C.G., Mitra D., Sharma A., Smith C.L., Hegde R.S. The efficiency of protein compartmentalization into the secretory pathway. Mol. Biol. Cell 2005, 16:279-291.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 279-291
    • Levine, C.G.1    Mitra, D.2    Sharma, A.3    Smith, C.L.4    Hegde, R.S.5
  • 31
    • 84869780364 scopus 로고    scopus 로고
    • SGTA antagonizes BAG6-mediated protein triage
    • Leznicki P., High S. SGTA antagonizes BAG6-mediated protein triage. Proc. Natl. Acad. Sci. USA 2012, 109:19214-19219.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 19214-19219
    • Leznicki, P.1    High, S.2
  • 32
    • 77954352789 scopus 로고    scopus 로고
    • Bat3 promotes the membrane integration of tail-anchored proteins
    • Leznicki P., Clancy A., Schwappach B., High S. Bat3 promotes the membrane integration of tail-anchored proteins. J.Cell Sci. 2010, 123:2170-2178.
    • (2010) J.Cell Sci. , vol.123 , pp. 2170-2178
    • Leznicki, P.1    Clancy, A.2    Schwappach, B.3    High, S.4
  • 34
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: a link between the chaperone and proteasome systems
    • McDonough H., Patterson C. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 2003, 8:303-308.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 35
    • 77957189436 scopus 로고    scopus 로고
    • ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum
    • Mehnert M., Sommer T., Jarosch E. ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum. Bioessays 2010, 32:905-913.
    • (2010) Bioessays , vol.32 , pp. 905-913
    • Mehnert, M.1    Sommer, T.2    Jarosch, E.3
  • 36
    • 33749642291 scopus 로고    scopus 로고
    • Mutation in the Trapalpha/Ssr1 gene, encoding translocon-associated protein alpha, results in outflow tract morphogenetic defects
    • Mesbah K., Camus A., Babinet C., Barra J. Mutation in the Trapalpha/Ssr1 gene, encoding translocon-associated protein alpha, results in outflow tract morphogenetic defects. Mol. Cell. Biol. 2006, 26:7760-7771.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7760-7771
    • Mesbah, K.1    Camus, A.2    Babinet, C.3    Barra, J.4
  • 37
  • 38
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • Orsi A., Fioriti L., Chiesa R., Sitia R. Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. J.Biol. Chem. 2006, 281:30431-30438.
    • (2006) J.Biol. Chem. , vol.281 , pp. 30431-30438
    • Orsi, A.1    Fioriti, L.2    Chiesa, R.3    Sitia, R.4
  • 39
    • 84873419140 scopus 로고    scopus 로고
    • The ribosome as a hub for protein quality control
    • Pechmann S., Willmund F., Frydman J. The ribosome as a hub for protein quality control. Mol. Cell 2013, 49:411-421.
    • (2013) Mol. Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 40
    • 10644267669 scopus 로고    scopus 로고
    • Protection from cytosolic prion protein toxicity by modulation of protein translocation
    • Rane N.S., Yonkovich J.L., Hegde R.S. Protection from cytosolic prion protein toxicity by modulation of protein translocation. EMBO J. 2004, 23:4550-4559.
    • (2004) EMBO J. , vol.23 , pp. 4550-4559
    • Rane, N.S.1    Yonkovich, J.L.2    Hegde, R.S.3
  • 41
    • 84869065405 scopus 로고    scopus 로고
    • Design principles of protein biosynthesis-coupled quality control
    • Rodrigo-Brenni M.C., Hegde R.S. Design principles of protein biosynthesis-coupled quality control. Dev. Cell 2012, 23:896-907.
    • (2012) Dev. Cell , vol.23 , pp. 896-907
    • Rodrigo-Brenni, M.C.1    Hegde, R.S.2
  • 42
  • 43
    • 84878857004 scopus 로고    scopus 로고
    • Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation
    • Shao S., von der Malsburg K., Hegde R.S. Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation. Mol. Cell 2013, 50:637-648.
    • (2013) Mol. Cell , vol.50 , pp. 637-648
    • Shao, S.1    von der Malsburg, K.2    Hegde, R.S.3
  • 44
    • 77954691102 scopus 로고    scopus 로고
    • Invitro dissection of protein translocation into the mammalian endoplasmic reticulum
    • Sharma A., Mariappan M., Appathurai S., Hegde R.S. Invitro dissection of protein translocation into the mammalian endoplasmic reticulum. Methods Mol. Biol. 2010, 619:339-363.
    • (2010) Methods Mol. Biol. , vol.619 , pp. 339-363
    • Sharma, A.1    Mariappan, M.2    Appathurai, S.3    Hegde, R.S.4
  • 45
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • Stefanovic S., Hegde R.S. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 2007, 128:1147-1159.
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 46
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Prot. Sci. 1998, 7:1029-1038.
    • (1998) Prot. Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 47
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • Wang F., Brown E.C., Mak G., Zhuang J., Denic V. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 2010, 40:159-171.
    • (2010) Mol. Cell , vol.40 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5
  • 48
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y. A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol. Cell 2011, 42:758-770.
    • (2011) Mol. Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5    Ye, Y.6
  • 49
    • 84871989736 scopus 로고    scopus 로고
    • E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation
    • Zhi X., Zhao D., Wang Z., Zhou Z., Wang C., Chen W., Liu R., Chen C. E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation. Cancer Res. 2013, 73:385-394.
    • (2013) Cancer Res. , vol.73 , pp. 385-394
    • Zhi, X.1    Zhao, D.2    Wang, Z.3    Zhou, Z.4    Wang, C.5    Chen, W.6    Liu, R.7    Chen, C.8
  • 50
    • 81855227611 scopus 로고    scopus 로고
    • Motility and segregation of Hsp104-associated protein aggregates in budding yeast
    • Zhou C., Slaughter B.D., Unruh J.R., Eldakak A., Rubinstein B., Li R. Motility and segregation of Hsp104-associated protein aggregates in budding yeast. Cell 2011, 147:1186-1196.
    • (2011) Cell , vol.147 , pp. 1186-1196
    • Zhou, C.1    Slaughter, B.D.2    Unruh, J.R.3    Eldakak, A.4    Rubinstein, B.5    Li, R.6
  • 51
    • 33751185584 scopus 로고    scopus 로고
    • Protein transport into the endoplasmic reticulum: mechanisms and pathologies
    • Zimmermann R., Müller L., Wullich B. Protein transport into the endoplasmic reticulum: mechanisms and pathologies. Trends Mol. Med. 2006, 12:567-573.
    • (2006) Trends Mol. Med. , vol.12 , pp. 567-573
    • Zimmermann, R.1    Müller, L.2    Wullich, B.3


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