Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response

Trends in Immunology

Volumn 25, Issue 1, 2004, Pages 17-24

  Gass, Jennifer N ^a   Gunn, Kathryn E ^a   Sriburi, Rungtawan ^a   Brewer, Joseph W ^a  

^a LOYOLA UNIVERSITY CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; ANTIBODY; CHAPERONE; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; PANCREATIC ELONGATION INITIATION FACTOR 2ALPHA KINASE; PROTEIN; PROTEIN IRE1; PROTEIN SERINE THREONINE KINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1;

ANTIBODY PRODUCTION; ANTIBODY RESPONSE; B LYMPHOCYTE; B LYMPHOCYTE DIFFERENTIATION; CELL DIFFERENTIATION; CELL MATURATION; CELL TYPE; ENDOPLASMIC RETICULUM; GENE CONTROL; HUMORAL IMMUNITY; IMMUNOGLOBULIN PRODUCTION; NONHUMAN; PLASMA CELL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN FOLDING; REGULATORY MECHANISM; REVIEW; RNA SPLICING; RNA TRANSLATION; SECRETORY CELL; SIGNAL TRANSDUCTION; STRESS;

EID: 0346331895     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2003.11.004     Document Type: Review

References (64)

1. Calame K.L., et al. Regulatory mechanisms that determine the development and function of plasma cells. Annu. Rev. Immunol. 21:2003;205-230.
2. -/- mice reveals a role for translational control in secretory cell survival. Mol. Cell. 7:2001;1153-1163.
3. Zhang P., et al. The PERK eukaryotic initiation factor 2 α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol. Cell. Biol. 22:2002;3864-3874.
4. Harding H.P., et al. Transcriptional and translational control in the mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18:2002;575-599.
5. Lewis M.J., et al. Structure and assembly of the endoplasmic reticulum. The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes. J. Biol. Chem. 260:1985;3050-3057.
6. Wiest D.L., et al. Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately. J. Cell Biol. 110:1990;1501-1511.
7. Reimold A.M., et al. Plasma cell differentiation requires the transcription factor XBP-1. Nature. 412:2001;300-307.
8. Yoshida H., et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell. 107:2001;881-891.
9. Shen X., et al. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell. 107:2001;893-903.
10. Calfon M., et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature. 415:2002;92-96.
11. Lee K., et al. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 16:2002;452-466.
12. Iwakoshi N.N., et al. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat. Immunol. 4:2003;321-329.
13. Takagaki Y., Manley J.L. Levels of polyadenylation factor CstF-64 control IgM heavy chain mRNA accumulation and other events associated with B cell differentiation. Mol. Cell. 2:1998;761-771.
14. Phillips C., et al. Regulation of nuclear poly(A) addition controls the expression of immunoglobulin M secretory mRNA. EMBO J. 20:2001;6443-6452.
15. Gass J.N., et al. Activation of an unfolded protein response during differentiation of antibody-secreting B cells. J. Biol. Chem. 277:2002;49047-49054.
16. Stevens F.J., Argon Y. Protein folding in the ER. Semin. Cell Dev. Biol. 10:1999;443-454.
17. Ellgaard L., Helenius A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4:2003;181-191.
18. Rush J.S., et al. Biogenesis of the endoplasmic reticulum in activated B lymphocytes: temporal relationships between the induction of protein N-glycosylation activity and the biosynthesis of membrane protein and phospholipid. Arch. Biochem. Biophys. 284:1991;63-70.
19. Kozutsumi Y., et al. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature. 332:1988;462-464.
20. Patil C., Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 13:2001;349-355.
21. Ma Y., Hendershot L.M. The unfolding tale of the unfolded protein response. Cell. 107:2001;827-830.
22. Bertolotti A., et al. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2:2000;326-332.
23. Shen J., et al. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell. 3:2002;99-111.
24. Haze K., et al. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell. 10:1999;3787-3799.
25. Haze K., et al. Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response. Biochem. J. 355:2001;19-28.
26. Ye J., et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell. 6:2000;1355-1364.
27. Brown M.S., Goldstein J.L. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell. 89:1997;331-340.
28. Yoshida H., et al. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273:1998;33741-33749.
29. Roy B., Lee A.S. The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex. Nucleic Acids Res. 27:1999;1437-1443.
30. Yoshida H., et al. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20:2000;6755-6767.
31. Tirasophon W., et al. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12:1998;1812-1824.
32. Wang X.Z., et al. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 17:1998;5708-5717.
33. Bertolotti A., et al. Increased sensitivity to dextran sodium sulfate colitis in IRE1β-deficient mice. J. Clin. Invest. 107:2001;585-593.
34. Lee A.-H., et al. Proteasome inhibitors disrupt the unfolded response in myeloma cells. Proc. Natl. Acad. Sci. U. S. A. 100:2003;9946-9951.
35. Shi Y., et al. Identification and characterization of pancreatic eukaryotic initiation factor 2 α-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18:1998;7499-7509.
36. Harding H.P., et al. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature. 397:1999;271-274.
37. Harding H.P., et al. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell. 5:2000;897-904.
38. Novoa I., et al. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α J. Cell Biol. 153:2001;1011-1022.
39. Novoa I., et al. Stress-induced gene expression requires programmed recovery from translational repression. EMBO J. 22:2003;1180-1187.
40. Brush M.H., et al. Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 α to the endoplasmic reticulum and promotes dephosphorylation of the α subunit of eukaryotic translation initiation factor 2. Mol. Cell. Biol. 23:2003;1292-1303.
41. Yan W., et al. Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc. Natl. Acad. Sci. U. S. A. 99:2002;15920-15925.
42. van Huizen R., et al. P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2α signaling. J. Biol. Chem. 278:2003;15558-15564.
43. Harding H.P., et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell. 6:2000;1099-1108.
44. Ma Y., Hendershot L.M. Delineation of the negative feedback regulatory loop that controls protein translation during ER stress. J. Biol. Chem. 278:2003;34864-34873.
45. Harding H.P., et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell. 11:2003;619-633.
46. Zinszner H., et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev. 12:1998;982-995.
47. Urano F., et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science. 287:2000;664-666.
48. Reimold A.M., et al. An essential role in liver development for transcription factor XBP-1. Genes Dev. 14:2000;152-157.
49. Scheuner D., et al. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol. Cell. 7:2001;1165-1176.
50. Delepine M., et al. EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat. Genet. 25:2000;406-409.
51. Wolcott C.D., Rallison M.L. Infancy-onset diabetes mellitus and multiple epiphyseal dysplasia. J. Pediatr. 80:1972;292-297.
52. van Anken E., et al. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity. 18:2003;243-253.
53. Lee Y.K., et al. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol. Biol. Cell. 10:1999;2209-2219.
54. Hellman R., et al. The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J. Cell Biol. 144:1999;21-30.
55. Turner C.A., et al. Blimp-1, a novel zinc finger-containing protein that can drive the maturation of B lymphocytes into immunoglobulin-secreting cells. Cell. 77:1994;297-306.
56. Calame K.L. Plasma cells: finding new light at the end of B cell development. Nat. Immunol. 2:2001;1103-1108.
57. Lin K.-I., et al. Blimp-1-dependent repression of Pax-5 is required for differentiation of B cells to immunoglobulin M-secreting plasma cells. Mol. Cell. Biol. 22:2002;4771-4780.
58. Yoneda T., et al. Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J. Biol. Chem. 276:2001;13935-13940.
59. Morishima N., et al. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J. Biol. Chem. 277:2002;34287-34294.
60. Yoshida H., et al. Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6α and 6β that activates the mammalian unfolded protein response. Mol. Cell. Biol. 21:2001;1239-1248.
61. Marcu M.G., et al. Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1α Mol. Cell. Biol. 22:2002;8506-8513.
62. Brewer J.W., Diehl J.A. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc. Natl. Acad. Sci. U. S. A. 97:2000;12625-12630.
63. Hampton R.Y. ER stress response: getting the UPR hand on misfolded proteins. Curr. Biol. 10:2000;R518-R521.
64. Reimold A.M., et al. Transcription factor B cell lineage-specific activator protein regulates the gene for human X-box binding protein 1. J. Exp. Med. 183:1996;393-401.