DOI: 10.4049/jimmunol.164.9.4713. Accelerated Proteasomal Degradation of Membrane Ig Heavy Chains

Accelerated Proteasomal Degradation of Membrane Ig Heavy Chains
10.4049/jimmunol.164.9.4713
Crossref journal-article
Oxford University Press (OUP)
The Journal of Immunology (286)
Abstract
AbstractMembrane IgG H chains turn over considerably more rapidly than secretory Ig H chains in the 18-81 A2 pre-B cell line. This rapid degradation occurs in proteasomes. N-Glycosylated membrane Ig H chains accumulate in the endoplasmic reticulum in the presence of proteasomal inhibitors, suggesting that retrotranslocation and proteasomal degradation of membrane Ig H chains may be closely coupled processes. Accelerated proteasomal degradation of membrane Ig H chains was also observed in transfected nonlymphoid cells. At steady state, the membrane form of the H chain associates more readily with Bip and calnexin than its secretory counterpart. The preferential recognition of membrane, as opposed to secretory, Ig H chains by some endoplasmic reticulum chaperones, may provide an explanation for the accelerated proteasomal degradation of the former.
Bibliography
Ho, S. C., Chaudhuri, S., Bachhawat, A., McDonald, K., & Pillai, S. (2000). Accelerated Proteasomal Degradation of Membrane Ig Heavy Chains. The Journal of Immunology, 164(9), 4713â4719.
Authors 5
Siew C. Ho (first)
Subhra Chaudhuri (additional)
Anand Bachhawat (additional)
Kenneth McDonald (additional)
Shiv Pillai (additional)
References 53 Referenced 11
Dates
Type	When
Created	11 years, 4 months ago (April 21, 2014, 10:34 p.m.)
Deposited	8 months ago (Jan. 2, 2025, 1:04 p.m.)
Indexed	8 months ago (Jan. 3, 2025, 12:33 a.m.)
Issued	25 years, 4 months ago (May 1, 2000)
Published	25 years, 4 months ago (May 1, 2000)
Published Print	25 years, 4 months ago (May 1, 2000)
Funders 0
None
BibTeX
@article{Ho_2000, title={Accelerated Proteasomal Degradation of Membrane Ig Heavy Chains}, volume={164}, ISSN={1550-6606}, url={http://dx.doi.org/10.4049/jimmunol.164.9.4713}, DOI={10.4049/jimmunol.164.9.4713}, number={9}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Ho, Siew C. and Chaudhuri, Subhra and Bachhawat, Anand and McDonald, Kenneth and Pillai, Shiv}, year={2000}, month=may, pages={4713–4719} }
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  "abstract": "<jats:title>Abstract</jats:title><jats:p>Membrane IgG H chains turn over considerably more rapidly than secretory Ig H chains in the 18-81 A2 pre-B cell line. This rapid degradation occurs in proteasomes. N-Glycosylated membrane Ig H chains accumulate in the endoplasmic reticulum in the presence of proteasomal inhibitors, suggesting that retrotranslocation and proteasomal degradation of membrane Ig H chains may be closely coupled processes. Accelerated proteasomal degradation of membrane Ig H chains was also observed in transfected nonlymphoid cells. At steady state, the membrane form of the H chain associates more readily with Bip and calnexin than its secretory counterpart. The preferential recognition of membrane, as opposed to secretory, Ig H chains by some endoplasmic reticulum chaperones, may provide an explanation for the accelerated proteasomal degradation of the former.</jats:p>",
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      "unstructured": "Wiertz, E. J. H. J., D. Tortorella, M. Bogyo, J. Yu, W. Mothes, T. R. Jones, T. A. Rapoport, H. L. Ploegh. 1996. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature\u2008384: 432",
      "DOI": "10.1038/384432a0"
    },
    {
      "key": "2022123115143847100_R2",
      "doi-asserted-by": "crossref",
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    {
      "key": "2022123115143847100_R3",
      "doi-asserted-by": "crossref",
      "unstructured": "Brodsky, J. L., A. A. McCracken. 1997. ER associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol.\u20087: 151",
      "DOI": "10.1016/S0962-8924(97)01020-9"
    },
    {
      "key": "2022123115143847100_R4",
      "doi-asserted-by": "crossref",
      "unstructured": "Hiller, M. H., A. Finger, M. Schweiger, D. H. Wolf. 1996. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science\u2008273: 1725",
      "DOI": "10.1126/science.273.5282.1725"
    },
    {
      "key": "2022123115143847100_R5",
      "doi-asserted-by": "crossref",
      "unstructured": "Jensen, T. J., M. A. Loo, S. Pind, D. B. Williams, A. L. Goldberg, J. R. Riordan. 1995. Multiple proteolytic systems including the proteasome contribute to CFTR processing. Cell\u200883: 129",
      "DOI": "10.1016/0092-8674(95)90241-4"
    },
    {
      "key": "2022123115143847100_R6",
      "doi-asserted-by": "crossref",
      "unstructured": "Huppa, J. B., H. L. Ploegh. 1997. The \u03b1 chain of the T cell antigen receptor is degraded in the cytosol. Immunity\u20087: 113",
      "DOI": "10.1016/S1074-7613(00)80514-2"
    },
    {
      "key": "2022123115143847100_R7",
      "doi-asserted-by": "crossref",
      "unstructured": "Hughes, E. A., C. Hammond, P. Cresswell. 1997. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. USA\u200894: 1896",
      "DOI": "10.1073/pnas.94.5.1896"
    },
    {
      "key": "2022123115143847100_R8",
      "doi-asserted-by": "crossref",
      "unstructured": "Johnston, J. A., C. L. Ward, R. R. Kopito. 1998. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol.\u2008143: 1883",
      "DOI": "10.1083/jcb.143.7.1883"
    },
    {
      "key": "2022123115143847100_R9",
      "doi-asserted-by": "crossref",
      "unstructured": "Yu, H., G. Guang, S. Kobayashi, R. R. Kopito. 1997. Cytosolic degradation of T-cell receptor \u03b1 chains by the proteasome. J. Biol. Chem.\u2008272: 20800",
      "DOI": "10.1074/jbc.272.33.20800"
    },
    {
      "key": "2022123115143847100_R10",
      "doi-asserted-by": "crossref",
      "unstructured": "Haas, I. G., M. Wabl. 1983. Immunoglobulin heavy chain binding protein. Nature\u2008306: 387",
      "DOI": "10.1038/306387a0"
    },
    {
      "key": "2022123115143847100_R11",
      "doi-asserted-by": "crossref",
      "unstructured": "Munro, S., H. R. Pelham. 1986. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell\u200846: 291",
      "DOI": "10.1016/0092-8674(86)90746-4"
    },
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      "key": "2022123115143847100_R12",
      "doi-asserted-by": "crossref",
      "unstructured": "Gething, M. J., K. McCammon, J. Sambrook. 1986. Expression of wild type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell\u200846: 939",
      "DOI": "10.1016/0092-8674(86)90076-0"
    },
    {
      "key": "2022123115143847100_R13",
      "doi-asserted-by": "crossref",
      "unstructured": "Degen, E., D. B. Williams. 1991. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. J. Cell Biol.\u2008112: 1099",
      "DOI": "10.1083/jcb.112.6.1099"
    },
    {
      "key": "2022123115143847100_R14",
      "doi-asserted-by": "crossref",
      "unstructured": "Hochstenbach, F., V. David, S. Watkins, M. B. Brenner. 1992. Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Natl. Acad. Sci. USA\u200889: 4734",
      "DOI": "10.1073/pnas.89.10.4734"
    },
    {
      "key": "2022123115143847100_R15",
      "doi-asserted-by": "crossref",
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      "DOI": "10.1073/pnas.89.18.8452"
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      "DOI": "10.1016/S0021-9258(18)55036-5"
    },
    {
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      "unstructured": "Ou, W.-J., P. H. Cameron, D. Y. Thomas, J. J. M. Bergeron. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature\u2008364: 771",
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    },
    {
      "key": "2022123115143847100_R18",
      "doi-asserted-by": "crossref",
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      "DOI": "10.1074/jbc.271.1.97"
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    {
      "key": "2022123115143847100_R19",
      "doi-asserted-by": "crossref",
      "unstructured": "Nash, P. D., M. Opas, M. Michalak. 1994. Calreticulin: not just another calcium-binding protein. Mol. Cell. Biochem.\u2008135: 71",
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      "doi-asserted-by": "crossref",
      "unstructured": "Plemper, R. K., S. Bohmler, J. Bordallo, T. Sommer, D. H. Wolf. 1997. Mutant analysis links the translocon and Bip to retrograde protein transport for ER degradation. Nature\u2008388: 891",
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    },
    {
      "key": "2022123115143847100_R21",
      "doi-asserted-by": "crossref",
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      "DOI": "10.1083/jcb.132.3.291"
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      "key": "2022123115143847100_R22",
      "doi-asserted-by": "crossref",
      "unstructured": "Hendershot, L. M., D. Bole, G. Kohler, J. F. Kearney. 1987. Assembly and secretion of heavy chains that do not associate post-translationally with Ig heavy chain binding protein. J. Cell Biol.\u2008104: 761",
      "DOI": "10.1083/jcb.104.3.761"
    },
    {
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      "DOI": "10.1016/0092-8674(93)90492-9"
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      "doi-asserted-by": "crossref",
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    },
    {
      "key": "2022123115143847100_R25",
      "doi-asserted-by": "crossref",
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    {
      "key": "2022123115143847100_R26",
      "doi-asserted-by": "crossref",
      "unstructured": "Hebert, D. N., B. Foellmer, A. Helenius. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell\u200881: 425",
      "DOI": "10.1016/0092-8674(95)90395-X"
    },
    {
      "key": "2022123115143847100_R27",
      "doi-asserted-by": "crossref",
      "unstructured": "Parodi, A., D. Mendelzon, G. Lederkremer, J. Martin-Barrientos. 1984. Evidence that transient glucosylation of protein-linked Man9GlcNAc2, Man8GlcNAc2 and Man7GlcNAc2 occurs in rat liver and Phaseolus vulgaris cells. J. Cell Biol.\u2008259: 6351",
      "DOI": "10.1016/S0021-9258(20)82148-6"
    },
    {
      "key": "2022123115143847100_R28",
      "doi-asserted-by": "crossref",
      "unstructured": "Helenius, A.. 1994. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell\u20085: 253",
      "DOI": "10.1091/mbc.5.3.253"
    },
    {
      "key": "2022123115143847100_R29",
      "doi-asserted-by": "crossref",
      "unstructured": "Zapun, A., S. M. Petrescu, P. M. Rudd, R. A. Dwek, D. Y. Thomas, J. J. M. Bergeron. 1997. Conformation independent binding of monoglucosylated ribonuclease B to calnexin. Cell\u200888: 29",
      "DOI": "10.1016/S0092-8674(00)81855-3"
    },
    {
      "key": "2022123115143847100_R30",
      "doi-asserted-by": "crossref",
      "unstructured": "Rodan, A. R., J. F. Simons, E. S. Trombetta, A. Helenius. 1996. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J.\u200824: 6921",
      "DOI": "10.1002/j.1460-2075.1996.tb01084.x"
    },
    {
      "key": "2022123115143847100_R31",
      "doi-asserted-by": "crossref",
      "unstructured": "Cannon, K. S., D. N. Hebert, A. Helenius. 1996. Glycan dependent and independent association of vesicular stomatitis virus G protein with calnexin. J. Biol. Chem.\u2008271: 14280",
      "DOI": "10.1074/jbc.271.24.14280"
    },
    {
      "key": "2022123115143847100_R32",
      "doi-asserted-by": "crossref",
      "unstructured": "Grupp, S. A., R. N. Mitchell, K. L. Schreiber, D. J. McKean, A. K. Abbas. 1995. Molecular mechanisms that control expression of the B lymphocyte antigen receptor complex. J. Exp. Med.\u2008181: 161",
      "DOI": "10.1084/jem.181.1.161"
    },
    {
      "key": "2022123115143847100_R33",
      "doi-asserted-by": "crossref",
      "unstructured": "Wu, Y., C. Pun, N. Hozumi. 1997. Roles of calnexin and Ig-Ab interactions with membrane Igs in the surface expression of the B cell antigen receptor of the IgM and IgD classes. J. Immunol.\u2008158: 2762",
      "DOI": "10.4049/jimmunol.158.6.2762"
    },
    {
      "key": "2022123115143847100_R34",
      "doi-asserted-by": "crossref",
      "unstructured": "O\u2019Hare, T., G. D. Wiens, E. A. Whitcomb, C. A. Enns, M. B. Rittenberg. 1999. Proteasome involvement in the degradation of unassembled Ig light chains. J. Immunol.\u2008163: 11",
      "DOI": "10.4049/jimmunol.163.1.11"
    },
    {
      "key": "2022123115143847100_R35",
      "doi-asserted-by": "crossref",
      "unstructured": "Bachhawat, A., S. Pillai. 1991. Distinct intracellular fates of membrane and secretory immunoglobulin heavy chains in a pre-B cell line. J. Cell Biol.\u2008115: 619",
      "DOI": "10.1083/jcb.115.3.619"
    },
    {
      "key": "2022123115143847100_R36",
      "doi-asserted-by": "crossref",
      "unstructured": "Morgenstern, J. P., H. Land. 1990. A series of mammalian expression vectors and characterization of their expression of a reporter gene in stably and transient transfected cells. Nucleic Acids Res.\u200818: 1068",
      "DOI": "10.1093/nar/18.4.1068"
    },
    {
      "key": "2022123115143847100_R37",
      "doi-asserted-by": "crossref",
      "unstructured": "Brewer, C. B., M. G. Roth. 1991. A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J. Cell Biol.\u2008114: 413",
      "DOI": "10.1083/jcb.114.3.413"
    },
    {
      "key": "2022123115143847100_R38",
      "doi-asserted-by": "crossref",
      "unstructured": "Lopata, M. A., D. W. Cleveland, B. Sollner-Webb. 1984. High level expression of a chloramphenicol acetyltransferase gene by DNA dextran mediated DNA transfection coupled with a dimethyl sulfoxide or glycerol shock treatment. Nucleic Acids Res.\u200812: 5707",
      "DOI": "10.1093/nar/12.14.5707"
    },
    {
      "key": "2022123115143847100_R39",
      "unstructured": "Chen, C., H. Okayama. 1988. Calcium phosphate mediated gene transfer: a highly efficient system for stably transforming cells with plasmid DNA. BioTechniques\u20086: 632"
    },
    {
      "key": "2022123115143847100_R40",
      "doi-asserted-by": "crossref",
      "unstructured": "Bogyo, M., J. S. McMaster, M. Gaczynska, D. Tortorella, A. L. Goldberg, M. Ploegh. 1997. Covalent modification of the active site threonine of the proteasomal \u03b2 subunits and the Escherichia\u2008coli homolog HslV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA\u200894: 6629",
      "DOI": "10.1073/pnas.94.13.6629"
    },
    {
      "key": "2022123115143847100_R41",
      "doi-asserted-by": "crossref",
      "unstructured": "Shamu, C. E., C. M. Story, T. A. Rapoport, H. L. Ploegh. 1999. The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate. J. Cell Biol.\u2008147: 45",
      "DOI": "10.1083/jcb.147.1.45"
    },
    {
      "key": "2022123115143847100_R42",
      "doi-asserted-by": "crossref",
      "unstructured": "Linnik, K. M., H. Herscovitz. 1998. Multiple molecular chaperones interact with apolipoprotein B during its maturation. J. Biol. Chem.\u2008273: 21368",
      "DOI": "10.1074/jbc.273.33.21368"
    },
    {
      "key": "2022123115143847100_R43",
      "doi-asserted-by": "crossref",
      "unstructured": "Chen, Y., F. Le Caherec, S. L. Chuck. 1998. Calnexin and other factors that alter translocation affect the rapid binding of ubiquitin to ApoB in the Sec 61 complex. J. Biol. Chem.\u2008273: 11887",
      "DOI": "10.1074/jbc.273.19.11887"
    },
    {
      "key": "2022123115143847100_R44",
      "doi-asserted-by": "crossref",
      "unstructured": "Keller, S. H., J. Lindstrom, P. Taylor. 1998. Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the \u03b1-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem.\u2008273: 17064",
      "DOI": "10.1074/jbc.273.27.17064"
    },
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      "key": "2022123115143847100_R45",
      "doi-asserted-by": "crossref",
      "unstructured": "Liu, Y., P. Choudhury, C. M. Cabral, R. N. Sifers. 1999. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. J. Biol. Chem.\u2008274: 5861",
      "DOI": "10.1074/jbc.274.9.5861"
    },
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      "key": "2022123115143847100_R46",
      "doi-asserted-by": "crossref",
      "unstructured": "Zhang, Q., M. Tector, R. D. Salter. 1995. Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules. J. Biol. Chem.\u2008270: 3944",
      "DOI": "10.1074/jbc.270.8.3944"
    },
    {
      "key": "2022123115143847100_R47",
      "doi-asserted-by": "crossref",
      "unstructured": "Arunachalam, B., P. Cresswell. 1995. Molecular requirements for the interaction of class II major histocompatibility complex molecules and invariant chain with calnexin. J. Biol. Chem.\u2008270: 2784",
      "DOI": "10.1074/jbc.270.6.2784"
    },
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      "key": "2022123115143847100_R48",
      "doi-asserted-by": "crossref",
      "unstructured": "Kim, P. S., P. Arvan. 1995. Calnexin and Bip act as sequential molecular chaperones during thyroglobulin folding in the ER. J. Cell Biol.\u2008128: 29",
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    },
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      "unstructured": "Loo, T. W., D. M. Clarke. 1994. Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis. J. Biol. Chem.\u2008269: 28683",
      "DOI": "10.1016/S0021-9258(19)61959-9"
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