AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
Endoplasmic reticulum-associated degradation (ERAD) disposes of aberrant proteins in the secretory pathway. Protein substrates of ERAD are dislocated via the Sec61p translocon from the endoplasmic reticulum to the cytosol, where they are ubiquitinated and degraded by the proteasome. Since the Sec61p...
Uložené v:
| Vydané v: | Molecular and cellular biology Ročník 22; číslo 2; s. 626 |
|---|---|
| Hlavní autori: | , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
| Vydavateľské údaje: |
United States
01.01.2002
|
| Predmet: | |
| ISSN: | 0270-7306 |
| On-line prístup: | Zistit podrobnosti o prístupe |
| Tagy: |
Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
|
| Abstract | Endoplasmic reticulum-associated degradation (ERAD) disposes of aberrant proteins in the secretory pathway. Protein substrates of ERAD are dislocated via the Sec61p translocon from the endoplasmic reticulum to the cytosol, where they are ubiquitinated and degraded by the proteasome. Since the Sec61p channel is also responsible for import of nascent proteins, this bidirectional passage should be coordinated, probably by molecular chaperones. Here we implicate the cytosolic chaperone AAA-ATPase p97/Cdc48p in ERAD. We show the association of mammalian p97 and its yeast homologue Cdc48p in complexes with two respective ERAD substrates, secretory immunoglobulin M in B lymphocytes and 6myc-Hmg2p in yeast. The membrane 6myc-Hmg2p as well as soluble lumenal CPY*, two short-lived ERAD substrates, are markedly stabilized in conditional cdc48 yeast mutants. The involvement of Cdc48p in dislocation is underscored by the accumulation of ERAD substrates in the endoplasmic reticulum when Cdc48p fails to function, as monitored by activation of the unfolded protein response. We propose that the role of p97/Cdc48p in ERAD, provided by its potential unfoldase activity and multiubiquitin binding capacity, is to act at the cytosolic face of the endoplasmic reticulum and to chaperone dislocation of ERAD substrates and present them to the proteasome. |
|---|---|
| AbstractList | Endoplasmic reticulum-associated degradation (ERAD) disposes of aberrant proteins in the secretory pathway. Protein substrates of ERAD are dislocated via the Sec61p translocon from the endoplasmic reticulum to the cytosol, where they are ubiquitinated and degraded by the proteasome. Since the Sec61p channel is also responsible for import of nascent proteins, this bidirectional passage should be coordinated, probably by molecular chaperones. Here we implicate the cytosolic chaperone AAA-ATPase p97/Cdc48p in ERAD. We show the association of mammalian p97 and its yeast homologue Cdc48p in complexes with two respective ERAD substrates, secretory immunoglobulin M in B lymphocytes and 6myc-Hmg2p in yeast. The membrane 6myc-Hmg2p as well as soluble lumenal CPY*, two short-lived ERAD substrates, are markedly stabilized in conditional cdc48 yeast mutants. The involvement of Cdc48p in dislocation is underscored by the accumulation of ERAD substrates in the endoplasmic reticulum when Cdc48p fails to function, as monitored by activation of the unfolded protein response. We propose that the role of p97/Cdc48p in ERAD, provided by its potential unfoldase activity and multiubiquitin binding capacity, is to act at the cytosolic face of the endoplasmic reticulum and to chaperone dislocation of ERAD substrates and present them to the proteasome.Endoplasmic reticulum-associated degradation (ERAD) disposes of aberrant proteins in the secretory pathway. Protein substrates of ERAD are dislocated via the Sec61p translocon from the endoplasmic reticulum to the cytosol, where they are ubiquitinated and degraded by the proteasome. Since the Sec61p channel is also responsible for import of nascent proteins, this bidirectional passage should be coordinated, probably by molecular chaperones. Here we implicate the cytosolic chaperone AAA-ATPase p97/Cdc48p in ERAD. We show the association of mammalian p97 and its yeast homologue Cdc48p in complexes with two respective ERAD substrates, secretory immunoglobulin M in B lymphocytes and 6myc-Hmg2p in yeast. The membrane 6myc-Hmg2p as well as soluble lumenal CPY*, two short-lived ERAD substrates, are markedly stabilized in conditional cdc48 yeast mutants. The involvement of Cdc48p in dislocation is underscored by the accumulation of ERAD substrates in the endoplasmic reticulum when Cdc48p fails to function, as monitored by activation of the unfolded protein response. We propose that the role of p97/Cdc48p in ERAD, provided by its potential unfoldase activity and multiubiquitin binding capacity, is to act at the cytosolic face of the endoplasmic reticulum and to chaperone dislocation of ERAD substrates and present them to the proteasome. Endoplasmic reticulum-associated degradation (ERAD) disposes of aberrant proteins in the secretory pathway. Protein substrates of ERAD are dislocated via the Sec61p translocon from the endoplasmic reticulum to the cytosol, where they are ubiquitinated and degraded by the proteasome. Since the Sec61p channel is also responsible for import of nascent proteins, this bidirectional passage should be coordinated, probably by molecular chaperones. Here we implicate the cytosolic chaperone AAA-ATPase p97/Cdc48p in ERAD. We show the association of mammalian p97 and its yeast homologue Cdc48p in complexes with two respective ERAD substrates, secretory immunoglobulin M in B lymphocytes and 6myc-Hmg2p in yeast. The membrane 6myc-Hmg2p as well as soluble lumenal CPY*, two short-lived ERAD substrates, are markedly stabilized in conditional cdc48 yeast mutants. The involvement of Cdc48p in dislocation is underscored by the accumulation of ERAD substrates in the endoplasmic reticulum when Cdc48p fails to function, as monitored by activation of the unfolded protein response. We propose that the role of p97/Cdc48p in ERAD, provided by its potential unfoldase activity and multiubiquitin binding capacity, is to act at the cytosolic face of the endoplasmic reticulum and to chaperone dislocation of ERAD substrates and present them to the proteasome. |
| Author | Diamant, Noam Kerem, Anat Rabinovich, Efrat Fröhlich, Kai-Uwe Bar-Nun, Shoshana |
| Author_xml | – sequence: 1 givenname: Efrat surname: Rabinovich fullname: Rabinovich, Efrat organization: Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel – sequence: 2 givenname: Anat surname: Kerem fullname: Kerem, Anat – sequence: 3 givenname: Kai-Uwe surname: Fröhlich fullname: Fröhlich, Kai-Uwe – sequence: 4 givenname: Noam surname: Diamant fullname: Diamant, Noam – sequence: 5 givenname: Shoshana surname: Bar-Nun fullname: Bar-Nun, Shoshana |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11756557$$D View this record in MEDLINE/PubMed |
| BookMark | eNo10DtPwzAUBWAPRbQUfgIoExNJbcePZAwVL6kIhjJHF_sagpI4tZOh_55IlOkun845uhdk0fseCblmNGOMF5vX7X3GecYzxVWqcpFxSvmCrCjXNNU5VUtyEeMPpVSVND8nS8a0VFLqFemrqkqr_TtETIZSb7bWiGK4SyAxx9FH3zYmMd8wYJgrk4CHqQloE-dDgr31Qwuxm0nAsTFTO3UpxOhNA-OMhuBHbPrE4lcAC2Pj-0ty5qCNeHW6a_Lx-LDfPqe7t6eXbbVLjZRiTHMHIgcqSkBBnbXgtGMMLSLPJVijHQVXKqXLQlmURnCJsnBcGi2U4Iavye1f7rzhMGEc666JBtsWevRTrDXLJaNazfDmBKfPDm09hKaDcKz_P8R_ATlOalM |
| CitedBy_id | crossref_primary_10_1104_pp_011742 crossref_primary_10_1091_mbc_e06_08_0696 crossref_primary_10_1016_j_febslet_2013_05_020 crossref_primary_10_1016_j_molcel_2010_11_033 crossref_primary_10_1016_j_brainres_2016_03_044 crossref_primary_10_1080_10409230590918685 crossref_primary_10_1093_hmg_ddw067 crossref_primary_10_1074_jbc_M501802200 crossref_primary_10_1091_mbc_e03_07_0506 crossref_primary_10_1073_pnas_1815495116 crossref_primary_10_1016_j_febslet_2011_09_032 crossref_primary_10_1007_s42764_019_00007_5 crossref_primary_10_1016_j_bbamcr_2013_06_031 crossref_primary_10_1016_S0968_0004_02_02125_4 crossref_primary_10_3390_genes14030676 crossref_primary_10_1371_journal_pone_0111505 crossref_primary_10_1016_j_bbamcr_2011_10_012 crossref_primary_10_1007_s00401_007_0224_7 crossref_primary_10_1371_journal_pone_0025061 crossref_primary_10_3390_ijms22041526 crossref_primary_10_1016_j_bbamcr_2011_09_005 crossref_primary_10_1073_pnas_2220340120 crossref_primary_10_1093_hmg_ddm037 crossref_primary_10_1016_j_bbamcr_2011_09_002 crossref_primary_10_1042_BCJ20160582 crossref_primary_10_1016_j_jprot_2018_09_014 crossref_primary_10_3109_10409238_2014_959889 crossref_primary_10_1002_1873_3468_12447 crossref_primary_10_1074_jbc_M110_179259 crossref_primary_10_1007_s00018_016_2238_6 crossref_primary_10_1016_j_cell_2014_07_050 crossref_primary_10_1242_jcs_072181 crossref_primary_10_1371_journal_pgen_1003210 crossref_primary_10_26508_lsa_202101022 crossref_primary_10_1016_j_jsb_2006_03_003 crossref_primary_10_1016_j_molcel_2018_03_016 crossref_primary_10_1091_mbc_01_08_0399 crossref_primary_10_1038_ncb1299 crossref_primary_10_3390_biom11071012 crossref_primary_10_1038_ncb1298 crossref_primary_10_1074_jbc_M405498200 crossref_primary_10_1111_j_1600_0854_2006_00460_x crossref_primary_10_1146_annurev_cellbio_18_032002_131219 crossref_primary_10_1083_jcb_201906047 crossref_primary_10_1038_sj_emboj_7601350 crossref_primary_10_1186_1475_2859_11_103 crossref_primary_10_1111_j_1600_0854_2011_01182_x crossref_primary_10_1371_journal_ppat_1000869 crossref_primary_10_1560_DA1X_C4K6_K8F7_RG5F crossref_primary_10_1038_srep46324 crossref_primary_10_1007_s00344_011_9216_x crossref_primary_10_1002_prot_25164 crossref_primary_10_1016_j_molcel_2011_05_010 crossref_primary_10_1074_jbc_M407837200 crossref_primary_10_1016_j_cell_2015_11_053 crossref_primary_10_1016_j_jsb_2006_02_015 crossref_primary_10_1038_emboj_2009_359 crossref_primary_10_7554_eLife_89606 crossref_primary_10_1007_s00018_022_04528_3 crossref_primary_10_1016_j_yexcr_2014_07_025 crossref_primary_10_3109_10409238_2015_1081869 crossref_primary_10_1016_j_nmd_2011_05_008 crossref_primary_10_1038_emboj_2009_231 crossref_primary_10_1126_scitranslmed_aam7996 crossref_primary_10_1091_mbc_e02_06_0363 crossref_primary_10_3390_ijms23169398 crossref_primary_10_1016_j_yexcr_2007_07_006 crossref_primary_10_1371_journal_pone_0041119 crossref_primary_10_1074_jbc_M112_417576 crossref_primary_10_1074_jbc_M208422200 crossref_primary_10_1016_j_ceb_2018_04_004 crossref_primary_10_1080_15384101_2020_1754584 crossref_primary_10_1083_jcb_201802018 crossref_primary_10_1104_pp_106_081703 crossref_primary_10_1111_j_1365_3083_2006_01747_x crossref_primary_10_1111_j_1365_313X_2010_04413_x crossref_primary_10_1089_dna_2014_2452 crossref_primary_10_1016_j_bbamcr_2005_03_011 crossref_primary_10_1002_1873_3468_13213 crossref_primary_10_1146_annurev_biochem_081111_125123 crossref_primary_10_1007_s12031_011_9635_y crossref_primary_10_1534_genetics_112_140467 crossref_primary_10_1083_jcb_200210086 crossref_primary_10_1073_pnas_0505006102 crossref_primary_10_1242_jcs_03163 crossref_primary_10_1146_annurev_pharmtox_45_120403_100127 crossref_primary_10_1016_j_molcel_2005_08_015 crossref_primary_10_1007_s13277_012_0631_9 crossref_primary_10_1038_cddis_2013_171 crossref_primary_10_1038_sj_emboj_7601307 crossref_primary_10_1093_cvr_cvp287 crossref_primary_10_1091_mbc_02_07_0115 crossref_primary_10_1081_DMR_120023683 crossref_primary_10_15252_embj_201489039 crossref_primary_10_1074_jbc_M113_475905 crossref_primary_10_1038_cr_2011_75 crossref_primary_10_1042_BCJ20160237 crossref_primary_10_1016_j_semcdb_2023_08_002 crossref_primary_10_1016_S0960_9822_02_00862_X crossref_primary_10_3390_genes13060963 crossref_primary_10_1152_physrev_00027_2011 crossref_primary_10_1007_s00424_010_0893_2 crossref_primary_10_1093_nar_gkr885 crossref_primary_10_1074_jbc_M409034200 crossref_primary_10_1002_pmic_200401085 crossref_primary_10_1038_nsmb_2793 crossref_primary_10_1074_jbc_M303360200 crossref_primary_10_1038_s42003_023_04763_9 crossref_primary_10_1016_S1096_7176_03_00030_2 crossref_primary_10_1074_jbc_M707366200 crossref_primary_10_3390_biom13050737 crossref_primary_10_1172_JCI61126 crossref_primary_10_1016_j_apsb_2019_11_002 crossref_primary_10_1016_j_molcel_2015_06_010 crossref_primary_10_1016_j_cellsig_2016_11_015 crossref_primary_10_1016_j_semcdb_2007_09_007 crossref_primary_10_1128_JVI_02039_06 crossref_primary_10_1016_j_semcdb_2007_09_008 crossref_primary_10_1186_s13024_023_00639_y crossref_primary_10_1074_jbc_M111_332882 crossref_primary_10_1016_j_bbadis_2008_09_003 crossref_primary_10_1074_jbc_M809282200 crossref_primary_10_1016_j_orthres_2004_12_012 crossref_primary_10_4161_cc_11_6_19446 crossref_primary_10_1016_j_semcdb_2007_09_002 crossref_primary_10_1038_ncb1554 crossref_primary_10_1002_yea_1071 crossref_primary_10_1242_jcs_093849 crossref_primary_10_1186_1742_4690_3_43 crossref_primary_10_1093_jb_mvy057 crossref_primary_10_1016_j_jpet_2025_103524 crossref_primary_10_1016_j_abb_2007_04_010 crossref_primary_10_1038_nrm4073 crossref_primary_10_1073_pnas_1905641117 crossref_primary_10_1074_jbc_M309938200 crossref_primary_10_1371_journal_ppat_1004295 crossref_primary_10_1093_brain_awq222 crossref_primary_10_1016_j_freeradbiomed_2017_03_031 crossref_primary_10_3389_fgene_2016_00073 crossref_primary_10_1016_j_molcel_2010_12_017 crossref_primary_10_1016_j_cell_2004_11_013 crossref_primary_10_1186_1475_2859_13_23 crossref_primary_10_1007_s00223_019_00520_5 crossref_primary_10_1016_j_ceb_2014_04_008 crossref_primary_10_1083_jcb_200307025 crossref_primary_10_1073_pnas_2505710122 crossref_primary_10_1074_jbc_M509700200 crossref_primary_10_1042_BJ20120662 crossref_primary_10_1074_jbc_M115_680215 crossref_primary_10_1242_jcs_176537 crossref_primary_10_1016_j_cbpc_2022_109271 crossref_primary_10_1016_S0014_5793_03_00723_3 crossref_primary_10_1111_j_1744_7917_2011_01485_x crossref_primary_10_1038_s41375_018_0355_y crossref_primary_10_1038_s41467_020_20796_8 crossref_primary_10_1074_jbc_M709316200 crossref_primary_10_7554_eLife_89606_3 crossref_primary_10_1074_jbc_M113_492199 crossref_primary_10_1038_sj_emboj_7601009 crossref_primary_10_1074_jbc_M303869200 crossref_primary_10_1111_j_1399_0004_2007_00887_x crossref_primary_10_1083_jcb_201110067 crossref_primary_10_1016_j_biocel_2013_01_006 crossref_primary_10_1073_pnas_0900742106 crossref_primary_10_1016_j_bbadis_2014_08_007 crossref_primary_10_1073_pnas_2135500100 crossref_primary_10_1016_j_bbamcr_2018_04_006 crossref_primary_10_1111_j_1365_2443_2009_01286_x crossref_primary_10_1074_jbc_M113_534529 crossref_primary_10_1073_pnas_1300328110 crossref_primary_10_1074_jbc_M113_482018 crossref_primary_10_1093_toxsci_kfz164 crossref_primary_10_1097_01_wad_0000183081_76820_5a crossref_primary_10_1074_jbc_M602248200 crossref_primary_10_1016_j_jbc_2022_102406 crossref_primary_10_3390_ijms12129057 crossref_primary_10_1097_MNH_0000000000000438 crossref_primary_10_1016_j_semcancer_2006_11_006 crossref_primary_10_1038_ncb0805_742 crossref_primary_10_1371_journal_pone_0117779 crossref_primary_10_1016_j_semcdb_2010_02_007 crossref_primary_10_1074_jbc_M115_656660 crossref_primary_10_1073_pnas_1707974114 crossref_primary_10_1083_jcb_200309132 crossref_primary_10_1111_j_0105_2896_2005_00318_x crossref_primary_10_1371_journal_pone_0076088 crossref_primary_10_1074_jbc_M116_737783 crossref_primary_10_1016_j_jsb_2006_04_003 crossref_primary_10_1016_j_molcel_2010_10_001 crossref_primary_10_15252_embj_2021109845 crossref_primary_10_1128_MCB_01362_12 crossref_primary_10_3390_biom4030774 crossref_primary_10_1242_jcs_260930 crossref_primary_10_1007_s10863_007_9120_z crossref_primary_10_15252_embj_201593106 crossref_primary_10_1074_jbc_M510592200 crossref_primary_10_1016_j_molcel_2007_09_012 crossref_primary_10_1080_10409238_2020_1784085 crossref_primary_10_1016_j_nbd_2024_106517 crossref_primary_10_1038_ng1332 crossref_primary_10_1523_JNEUROSCI_5397_12_2013 crossref_primary_10_1038_nsb972 crossref_primary_10_1074_jbc_M207783200 crossref_primary_10_1111_jipb_12372 crossref_primary_10_1038_nrm807 crossref_primary_10_1038_ncb0805_766 crossref_primary_10_1042_BJ20130133 crossref_primary_10_1242_jcs_059758 crossref_primary_10_1152_ajprenal_00032_2025 crossref_primary_10_1016_j_bbagrm_2013_02_010 crossref_primary_10_1074_jbc_M406683200 crossref_primary_10_1242_jcs_011247 crossref_primary_10_7554_eLife_55596 crossref_primary_10_1242_jcs_102137 crossref_primary_10_1073_pnas_0602954103 crossref_primary_10_1083_jcb_201808024 crossref_primary_10_7554_eLife_50903 crossref_primary_10_3389_fmolb_2017_00033 crossref_primary_10_1080_17460441_2017_1329294 crossref_primary_10_1016_j_expneurol_2024_114778 crossref_primary_10_1093_glycob_cwn108 crossref_primary_10_1074_jbc_M301080200 crossref_primary_10_1016_j_molcel_2011_08_028 crossref_primary_10_1128_MCB_00434_16 crossref_primary_10_1074_jbc_M602989200 crossref_primary_10_1074_jbc_M701862200 crossref_primary_10_1038_nrm780 crossref_primary_10_3390_cells8091051 crossref_primary_10_1146_annurev_biochem_062917_012749 crossref_primary_10_3389_fmolb_2017_00039 crossref_primary_10_1074_jbc_M513552200 crossref_primary_10_1128_JVI_77_8_4731_4738_2003 crossref_primary_10_1016_j_bbamcr_2020_118788 crossref_primary_10_1091_mbc_e17_03_0184 crossref_primary_10_1016_S0092_8674_03_00815_8 crossref_primary_10_1002_bies_201200159 crossref_primary_10_1007_s00401_013_1224_4 crossref_primary_10_1016_j_bbrc_2006_04_160 crossref_primary_10_1111_j_1742_4658_2008_06858_x crossref_primary_10_1074_jbc_M705216200 crossref_primary_10_1128_MCB_00962_10 crossref_primary_10_1093_aob_mcy068 crossref_primary_10_1111_j_1365_2443_2008_01214_x crossref_primary_10_1186_1477_7827_9_117 crossref_primary_10_1016_j_str_2008_02_010 crossref_primary_10_1038_nature23314 crossref_primary_10_1091_mbc_e05_04_0375 crossref_primary_10_1083_jcb_201007013 crossref_primary_10_1016_j_gene_2016_02_042 crossref_primary_10_1016_j_yexmp_2004_08_006 crossref_primary_10_1016_j_aquaculture_2024_740938 crossref_primary_10_1016_j_jsb_2012_04_017 crossref_primary_10_1002_ana_20407 crossref_primary_10_1016_j_jmb_2005_01_060 crossref_primary_10_3390_toxins3070787 crossref_primary_10_1016_j_ceb_2012_05_010 crossref_primary_10_1111_cge_13095 crossref_primary_10_1038_sj_emboj_7601088 crossref_primary_10_1038_s41598_019_46949_4 crossref_primary_10_3390_ijms25126445 crossref_primary_10_1002_biof_5520280207 crossref_primary_10_1111_j_1600_0854_2010_01093_x crossref_primary_10_3390_ijms21155369 crossref_primary_10_1128_MCB_26_3_822_830_2006 crossref_primary_10_1186_s13023_025_03567_w crossref_primary_10_1074_jbc_M117_786376 crossref_primary_10_1186_1745_6150_1_8 crossref_primary_10_1016_j_critrevonc_2004_11_004 crossref_primary_10_1155_2017_2969271 crossref_primary_10_1093_hmg_ddq157 crossref_primary_10_1002_iub_520 crossref_primary_10_1089_ars_2007_1817 crossref_primary_10_1097_00005072_200606000_00005 crossref_primary_10_1074_jbc_M110_201400 crossref_primary_10_1074_jbc_RA119_007585 crossref_primary_10_1074_jbc_M110_177618 crossref_primary_10_2135_cropsci2011_10_0551 crossref_primary_10_1016_j_arr_2016_04_008 crossref_primary_10_1371_journal_pone_0058116 crossref_primary_10_1124_pr_117_015370 crossref_primary_10_1111_j_1600_0854_2004_00159_x crossref_primary_10_1016_j_neuron_2013_02_029 crossref_primary_10_1016_S0955_0674_02_00358_7 crossref_primary_10_1242_jcs_115_14_3007 crossref_primary_10_1158_1541_7786_MCR_06_0019 crossref_primary_10_1074_jbc_M110_174680 crossref_primary_10_1111_j_1742_4658_2006_05494_x crossref_primary_10_3390_ijms22042078 crossref_primary_10_1002_adhm_202001934 crossref_primary_10_1007_s00425_004_1447_7 crossref_primary_10_1074_jbc_M114_630061 crossref_primary_10_1016_j_tibs_2006_11_005 crossref_primary_10_1016_j_molcel_2019_10_003 crossref_primary_10_3390_ijms19103020 crossref_primary_10_1242_jcs_00439 crossref_primary_10_1517_17425255_4_2_123 crossref_primary_10_1016_j_bbamcr_2013_03_018 crossref_primary_10_1242_jcs_02732 crossref_primary_10_1074_jbc_M405935200 crossref_primary_10_1016_j_bbamcr_2011_07_001 crossref_primary_10_1016_j_jsb_2003_11_014 crossref_primary_10_1016_S1016_8478_23_13977_X crossref_primary_10_1016_j_nmd_2009_01_009 crossref_primary_10_1091_mbc_e06_05_0432 crossref_primary_10_1091_mbc_E15_06_0354 crossref_primary_10_1371_journal_pone_0172983 crossref_primary_10_3390_ijms25115633 crossref_primary_10_1534_genetics_109_111419 crossref_primary_10_1038_nrd4467 crossref_primary_10_1074_jbc_M708347200 crossref_primary_10_1016_j_bbamcr_2011_07_009 crossref_primary_10_1074_jbc_M113_521088 crossref_primary_10_1111_j_1365_2443_2010_01454_x crossref_primary_10_1091_mbc_E18_12_0754 crossref_primary_10_1038_nature02656 crossref_primary_10_1038_sj_emboj_7601974 crossref_primary_10_1074_jbc_M208730200 crossref_primary_10_1016_S0014_5793_03_01107_4 crossref_primary_10_1016_j_bbrc_2005_04_136 crossref_primary_10_1073_pnas_2414016122 crossref_primary_10_1177_1535370217697384 crossref_primary_10_1074_jbc_M204196200 crossref_primary_10_1083_jcb_200302169 crossref_primary_10_1016_j_nmd_2009_08_003 crossref_primary_10_1016_j_jchemneu_2003_08_007 crossref_primary_10_1371_journal_pone_0019225 crossref_primary_10_1242_jcs_217760 crossref_primary_10_1371_journal_pone_0148650 crossref_primary_10_1007_s10735_011_9374_y crossref_primary_10_1016_j_cell_2010_10_028 crossref_primary_10_1074_jbc_M508890200 crossref_primary_10_1091_mbc_e04_01_0024 crossref_primary_10_1016_j_brainres_2019_146532 crossref_primary_10_1371_journal_pbio_3001950 crossref_primary_10_15252_embj_201591888 crossref_primary_10_1111_j_1582_4934_2008_00462_x crossref_primary_10_1074_jbc_M111_302778 crossref_primary_10_1093_hmg_ddi426 crossref_primary_10_7554_eLife_56945 crossref_primary_10_1016_j_cell_2016_05_048 crossref_primary_10_1165_rcmb_2006_0365OC crossref_primary_10_1074_jbc_M307453200 crossref_primary_10_1038_nsmb_2111 crossref_primary_10_1074_jbc_M110_186981 crossref_primary_10_1016_j_cmet_2014_09_006 crossref_primary_10_1074_jbc_M402468200 crossref_primary_10_1016_j_bbrc_2010_03_005 crossref_primary_10_1016_j_nmd_2018_04_007 crossref_primary_10_1083_jcb_201312042 crossref_primary_10_1016_j_bbamcr_2008_01_023 crossref_primary_10_1091_mbc_e09_08_0743 crossref_primary_10_1007_s12031_011_9627_y crossref_primary_10_1091_mbc_e09_10_0910 crossref_primary_10_1083_jcb_200907055 crossref_primary_10_1007_s10719_008_9133_9 crossref_primary_10_1091_mbc_E18_02_0117 crossref_primary_10_1159_000072862 crossref_primary_10_1128_JB_185_6_1757_1767_2003 crossref_primary_10_1371_journal_pone_0022713 crossref_primary_10_1016_j_jsb_2014_05_010 crossref_primary_10_1078_0171_9335_00412 crossref_primary_10_1242_jcs_00817 crossref_primary_10_1016_j_jocn_2011_05_044 crossref_primary_10_1016_S0014_5793_02_02777_1 crossref_primary_10_1074_jbc_M110_158030 crossref_primary_10_1083_jcb_201008090 crossref_primary_10_1074_jbc_M705893200 crossref_primary_10_1016_j_bbrc_2012_07_080 crossref_primary_10_1073_pnas_1612988114 crossref_primary_10_1074_jbc_M801702200 crossref_primary_10_1016_j_ccell_2015_10_002 crossref_primary_10_1134_S1990750817010024 crossref_primary_10_1517_17425255_3_1_33 crossref_primary_10_1002_eji_200737743 crossref_primary_10_1111_j_1600_0854_2008_00729_x crossref_primary_10_1016_j_molcel_2006_03_036 crossref_primary_10_1016_j_cub_2006_11_013 crossref_primary_10_1034_j_1600_0854_2002_30803_x crossref_primary_10_1242_jcs_00841 crossref_primary_10_1111_j_1742_4658_2007_05639_x crossref_primary_10_1074_jbc_M113_469882 crossref_primary_10_1111_cts_12241 crossref_primary_10_1016_j_semcdb_2009_12_008 crossref_primary_10_1128_JVI_00286_18 crossref_primary_10_1016_j_bbamcr_2004_10_006 crossref_primary_10_1111_j_1365_2958_2004_04403_x crossref_primary_10_1042_BCJ20160760 crossref_primary_10_1371_journal_pone_0050490 |
| ContentType | Journal Article |
| DBID | CGR CUY CVF ECM EIF NPM 7X8 |
| DOI | 10.1128/MCB.22.2.626-634.2002 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | no_fulltext_linktorsrc |
| Discipline | Chemistry Biology |
| ExternalDocumentID | 11756557 |
| Genre | Research Support, U.S. Gov't, Non-P.H.S Research Support, Non-U.S. Gov't Journal Article |
| GroupedDBID | --- -DZ -~X .55 .GJ 0R~ 123 18M 29M 2WC 39C 3O- 4.4 53G 5RE 5VS 9M8 ABJNI ABRLO ABTAH ACGFO ACKIV ACNCT ADBBV ADIYS AENEX AEOZL AFFNX AGHSJ AGVNZ ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BTFSW C1A CGR CS3 CUY CVF DIK DU5 E3Z EBS ECM EIF EJD EMOBN F5P GX1 H13 HH5 HYE HZ~ IH2 KQ8 L7B M4Z MVM N9A NPM O9- OK1 P2P PKN RHF RHI RNS RPM RSF TDBHL TFL TFW TR2 UCJ UDS VQA W8F WH7 WHG WOQ X7M Y6R YIN YYP ZCA ZGI ZXP ZY4 7X8 AAGFI ADXHL TASJS |
| ID | FETCH-LOGICAL-c554t-3fa43a049ae40fddaf7f11edee235adc7f0af9667986de5c425e58f25c74642c2 |
| IEDL.DBID | 7X8 |
| ISICitedReferencesCount | 461 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000172983900022&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 0270-7306 |
| IngestDate | Wed Oct 01 17:09:58 EDT 2025 Wed Feb 19 02:32:15 EST 2025 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 2 |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c554t-3fa43a049ae40fddaf7f11edee235adc7f0af9667986de5c425e58f25c74642c2 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| OpenAccessLink | http://doi.org/10.1128/MCB.22.2.626-634.2002 |
| PMID | 11756557 |
| PQID | 71351076 |
| PQPubID | 23479 |
| ParticipantIDs | proquest_miscellaneous_71351076 pubmed_primary_11756557 |
| PublicationCentury | 2000 |
| PublicationDate | 2002-01-01 |
| PublicationDateYYYYMMDD | 2002-01-01 |
| PublicationDate_xml | – month: 01 year: 2002 text: 2002-01-01 day: 01 |
| PublicationDecade | 2000 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Molecular and cellular biology |
| PublicationTitleAlternate | Mol Cell Biol |
| PublicationYear | 2002 |
| SSID | ssj0006903 |
| Score | 2.275958 |
| Snippet | Endoplasmic reticulum-associated degradation (ERAD) disposes of aberrant proteins in the secretory pathway. Protein substrates of ERAD are dislocated via the... |
| SourceID | proquest pubmed |
| SourceType | Aggregation Database Index Database |
| StartPage | 626 |
| SubjectTerms | Adenosine Triphosphatases - metabolism Animals B-Lymphocytes - immunology B-Lymphocytes - metabolism Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Cell Line Cytosol - metabolism Endoplasmic Reticulum - metabolism Fungal Proteins - genetics Fungal Proteins - metabolism HMGB2 Protein - metabolism Immunoglobulin M - metabolism Macromolecular Substances Mice Molecular Chaperones - genetics Molecular Chaperones - metabolism Mutation Nuclear Proteins - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Valosin Containing Protein |
| Title | AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/11756557 https://www.proquest.com/docview/71351076 |
| Volume | 22 |
| WOSCitedRecordID | wos000172983900022&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV07T8MwED4BBcHC-_3ywIjb1E7qRkJCoQKxUHUAqVvl2mfRgTTQgtR_z9lJxIQYWDI5kuU7n7-7s78P4EomBpOujbhVTvAYI-RpZGNuO-0xeipKTF0Qm1D9fnc4TAdLcFO_hfHXKuuYGAK1nRpfI28FKTlKum-Ld-41o3xvtRLQWIaGJCDjfVoNf7jCKe8L_WWhIk5-3Kne71BAbj317ppCNEWT4DzvyFBbEb9jzHDWPGz9b5bbsFlhTJaVTrEDS5jvwlqpOrnYhfVeLfK2B3mWZTx7HtBZxopUtXrWxN3immlmFvPpzJMGM_OqPZt4juwD_b1htIyQLsPcTgvC3m80JDyF9HVEritz06BAATHJmfV8FKV00z68PNw_9x55JcHADeGMOZdOx1JTFqExjpy12inXbqNFFDLR1igXaUcZk0q7HYuJoQhApnciMSqmzMaIA1jJaYJHwIQbK2nGDoW2cdvpcZpiomItlcAEU3kMl_WSjmgRfN9C5zj9nI3qRT2Gw9Iqo6Jk4vBM5QRIE3Xy57-nsBF0XELx5AwajjY3nsOq-ZpPZh8XwXPo2x88fQPQ5848 |
| linkProvider | ProQuest |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=AAA-ATPase+p97%2FCdc48p%2C+a+cytosolic+chaperone+required+for+endoplasmic+reticulum-associated+protein+degradation&rft.jtitle=Molecular+and+cellular+biology&rft.au=Rabinovich%2C+Efrat&rft.au=Kerem%2C+Anat&rft.au=Fr%C3%B6hlich%2C+Kai-Uwe&rft.au=Diamant%2C+Noam&rft.date=2002-01-01&rft.issn=0270-7306&rft.volume=22&rft.issue=2&rft.spage=626&rft_id=info:doi/10.1128%2FMCB.22.2.626-634.2002&rft_id=info%3Apmid%2F11756557&rft_id=info%3Apmid%2F11756557&rft.externalDocID=11756557 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0270-7306&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0270-7306&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0270-7306&client=summon |