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

Journal of Cell Biology

Volumn 144, Issue 1, 1999, Pages 21-30

  Hellman, Rachel ^a   Vanhove, Marc ^a   Lejeune, Annabelle ^b   Stevens, Fred J ^c   Hendershot, Linda M ^a,d  

^a ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

^b UNIVERSITY OF LIÈGE   (Belgium)

^c ARGONNE NATIONAL LABORATORY   (United States)

^d UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

Author keywords

BiP; Chaperone; Endoplasmic reticulum; Protein folding

Indexed keywords

CHAPERONE; GLUCOSE REGULATED PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN;

ARTICLE; BINDING KINETICS; BINDING SITE; DISULFIDE BOND; ENDOPLASMIC RETICULUM; HUMAN; HUMAN CELL; HUMAN TISSUE; PREDICTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; SEQUENCE ANALYSIS; STOICHIOMETRY;

ADENOSINE TRIPHOSPHATASES; ANIMALS; BINDING SITES; CARRIER PROTEINS; COS CELLS; CYSTEINE; DISULFIDES; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; IMMUNOGLOBULIN CONSTANT REGIONS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN LAMBDA-CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR CHAPERONES; MUTATION; PROTEIN FOLDING; TUMOR CELLS, CULTURED;

MURINAE;

EID: 0033545187     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.1.21     Document Type: Article

References (43)

1. Alberini, C.M., P. Bet, C. Milstein, and R. Sitia. 1990. Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents. Nature. 347:485-487.
2. Amzel, L.M., and R.J. Poljak. 1979. Three-dimensional structure of immunoglobulins. Annu. Rev. Immunol. 48:961-997.
3. Bernard, O., N. Hozumi, and S. Tonegawa. 1978. Sequences of mouse immunoglobulin light chain genes before and after somatic changes. Cell. 15:1133-1144.
4. Blond-Elguindi, S., S.E. Cwirla, W.J. Dower, R.J. Lipshutz, S.R. Sprang, J.F. Sambrook, and M.J. Gething. 1993. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell. 75: 717-728.
5. Braakman, I., H. Hoover Litty, K.R. Wagner, and A. Helenius. 1991. Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114: 401-411.
6. Braakman, I., J. Helenius, and A. Helenius. 1992a. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO (Eur. Mol. Biol. Organ.) J. 11:1117-1722.
7. Braakman, I., J. Helenius, and A. Helenius. 1992b. Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature. 356:260-262.
8. Bukau, B., and A.L. Horwich. 1998. The Hsp70 and Hsp60 chaperone machines. Cell. 92:351-366.
9. Dorner, A.J., M.G. Krane, and R.J. Kaufman. 1988. Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells. Mol. Cell. Biol. 8:4063-4070.
10. Flynn, G.C., J. Pohl, M.T. Flocco, and J.E. Rothman. 1991. Peptide-binding specificity of the molecular chaperone BiP. Nature. 353:726-730.
11. Fra, A.M., C. Fagioli, D. Finazzi, R. Sitia, and C.M. Alberini. 1993. Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO (Eur. Mol. Biol. Organ.) J. 12:4755-4761.
12. Gaut, J.R., and L.M. Hendershot. 1993. Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain. J. Biol. Chem. 268: 7248-7255.
13. Gething, M.J., and J. Sambrook. 1992. Protein folding in the cell. Nature. 355: 33-45.
14. Gorlich, D., and T.A. Rapoport. 1993. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell. 75:615-630.
15. Goto, Y., and K. Hamaguchi. 1981. Formation of the intracham disulfide bond in the constant fragment of the immunoglobulin light chain. J. Mol. Biol. 146:321-340.
16. Goto, Y., and K. Hamaguchi. 1982. Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chain. J. Mol. Biol. 156:911-926.
17. Goto, Y., T. Azuma, and K. Hamaguchi. 1979. Refolding of the immunoglobulin light chain. J. Biochem. 85:1427-1438.
18. Graham, K.S., A. Le, and R.N. Sifers. 1990. Accumulation of the insoluble PiZ variant of human alpha 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP. J. Biol. Chem. 265: 20463-20468.
19. Haas, I.G. 1991. BiP - a heat shock protein involved in immunoglobulin chain assembly. Curr. Top. Microbiol. Immunol. 167:71-82.
20. Hamman, B.D., L.M. Hendershot, and A.E. Johnson. 1998. BiP maintains the permeability harrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell. 92:747-758.
21. Hammond, C., I. Braukman, and A. Helenius. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA. 91:913-917.
22. Hendershot, L., D. Bole, G. Kohler, and J.F. Kearney. 1987. Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein. J. Cell Biol. 104:761-767.
23. Hendershot, L.M., J. Y. Wei, J.R. Gaut, B. Lawson, P.J. Freiden, and K.G. Murti. 1995. In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum. Mol. Biol. Cell. 6:283-296.
24. Hendershot, L., J. Wei, J. Gaut, J. Melnick, S, Aviel, and Y. Argon. 1996. Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proc Natl. Acad. Sci. USA 93:5269-5274.
25. Hendrick, J.P., and F.U. Hartl. 1993. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Immunol. 62:349-384.
26. Ho, S.N., H.D. Hunt, R.M. Norton, J.K. Pullen, and L.R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:51-59.
27. Hurtley, S.M., D.G. Bole, H. Hoover Lilly, A. Heknius, and C.S. Copeland. 1989. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108:2117-2126.
28. Kaloff, C.R., and I.G. Haas. 1995. Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG. Immunity. 2:629-637.
29. Knarr, G., M.J. Gething, S. Modrow, and J. Buchner. 1995. BiP binding sequences in antibodies. J. Biol. Chem. 270:27589-27594.
30. Landry, S.J., R. Jordan, R. McMacken, and L.M. Gierasch. 1992. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature. 355:455-457.
31. Morris, J.A., A.J. Dorner, OA. Edwards, L.M. Hendershot, and R.J. Kaufman. 1997. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J Biol. Chem. 272:4327-4334.
32. Munro, S., and 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. 46:291-300.
33. Nicchitta, C.V., and G. Blobel. 1993. Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. Cell. 73: 989-998.
34. Palleros, D.R., K.L. Reid, L. Shi, W.J. Welch, and A.L. Fink. 1993. ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. Nature. 365:664-666.
35. Rudiger, S., L. Germeroth, J. Schneider-Mergener, and B. Bukau, 1997. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO (Eur. Mol. Biol. Organ.) J. 16:1501-1507.
36. Simons, J.F., S. Ferro-Novick, M.D. Rose, and A. Helenius. 1995. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell Biol 130:41-49.
37. Skowronek, M.H., L.M. Hendershot, and I.G. Haas. 1998. The variable domain of non-assembled Ig light chains determines both their half-life and binding to BiP. Proc. Natl. Acad. Sci. USA. 95:1574-1578.
38. Takenaka, I.M., S.M. Leung, S.J. McAndrew, J.P. Brown, and L.E. Hightower. 1995. Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences. J. Biol. Chem. 270:19839-19844.
39. Vanhove, M., S. Houba, J. Lamotte-Brasseur, and J.M. Frere. 1995. Probing the determinants of protein stability: comparison of class A beta-lactamases. Biochem. J. 308:859-864.
40. Vogel, J.P., L.M. Misra, and M.D. Rose. 1990. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110:1885-1895.
41. Walter, P., and A.E. Johnson. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10: 87-119.
42. Wei, J.-Y., and L.M. Hendershot. 1995. Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria. J. Biol. Chem. 270:26670-26676.
43. Wei, J.-Y., J.R. Gaut, and L.M. Hendershot. 1995. In vitro dissociation of BiP peptide complexes requires a conformational change in BiP after ATP binding hut does not require ATP hydrolysis. J. Biol. Chem. 270:26677-26682.