Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1994 Dec 2;127(6):1557–1574. doi: 10.1083/jcb.127.6.1557

Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells

PMCID: PMC2120279  PMID: 7798312

Abstract

The carboxyl-terminal Lys-Asp-Glu-Leu (KDEL), or a closely-related sequence, is important for ER localization of both lumenal as well as type II membrane proteins. This sequence functions as a retrieval signal at post-ER compartment(s), but the exact compartment(s) where the retrieval occurs remains unresolved. With an affinity-purified antibody against the carboxyl-terminal sequence of the mammalian KDEL receptor, we have investigated its subcellular localization using immunogold labeling on thawed cryosections of different tissues, such as mouse spermatids and rat pancreas, as well as HeLa, Vero, NRK, and mouse L cells. We show that rab1 is an excellent marker of the intermediate compartment, and we use this marker, as well as budding profiles of the mouse hepatitis virus (MHV) in cells infected with this virus, to identify this compartment. Our results demonstrate that the KDEL receptor is concentrated in the intermediate compartment, as well as in the Golgi stack. Lower but significant labeling was detected in the rough ER. In general, only small amounts of the receptor were detected on the trans side of the Golgi stack, including the trans- Golgi network (TGN) of normal cells and tissues. However, some stress conditions, such as infection with vaccinia virus or vesicular stomatitis virus, as well as 20 degrees C or 43 degrees C treatment, resulted in a significant shift of the distribution towards the trans- TGN side of the Golgi stack. This shift could be quantified in HeLa cells stably expressing a TGN marker. No significant labeling was detected in structures distal to the TGN under all conditions tested. After GTP gamma S treatment of permeabilized cells, the receptor was detected in the beta-COP-containing buds/vesicles that accumulate after this treatment, suggesting that these vesicles may transport the receptor between compartments. We propose that retrieval of KDEL- containing proteins occurs at multiple post-ER compartments up to the TGN along the exocytotic pathway, and that within this pathway, the amounts of the receptor in different compartments varies according to physiological conditions.

Full Text

The Full Text of this article is available as a PDF (8.8 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson R. G., Orci L. A view of acidic intracellular compartments. J Cell Biol. 1988 Mar;106(3):539–543. doi: 10.1083/jcb.106.3.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balch W. E. Biochemistry of interorganelle transport. A new frontier in enzymology emerges from versatile in vitro model systems. J Biol Chem. 1989 Oct 15;264(29):16965–16968. [PubMed] [Google Scholar]
  3. Balch W. E., Keller D. S. ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments. J Biol Chem. 1986 Nov 5;261(31):14690–14696. [PubMed] [Google Scholar]
  4. Balch W. E. Molecular dissection of early stages of the eukaryotic secretory pathway. Curr Opin Cell Biol. 1990 Aug;2(4):634–641. doi: 10.1016/0955-0674(90)90104-m. [DOI] [PubMed] [Google Scholar]
  5. Bowman E. J., Siebers A., Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci U S A. 1988 Nov;85(21):7972–7976. doi: 10.1073/pnas.85.21.7972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chaudhary V. K., Jinno Y., FitzGerald D., Pastan I. Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity. Proc Natl Acad Sci U S A. 1990 Jan;87(1):308–312. doi: 10.1073/pnas.87.1.308. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chavrier P., Parton R. G., Hauri H. P., Simons K., Zerial M. Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell. 1990 Jul 27;62(2):317–329. doi: 10.1016/0092-8674(90)90369-p. [DOI] [PubMed] [Google Scholar]
  8. Dean N., Pelham H. R. Recycling of proteins from the Golgi compartment to the ER in yeast. J Cell Biol. 1990 Aug;111(2):369–377. doi: 10.1083/jcb.111.2.369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Duden R., Griffiths G., Frank R., Argos P., Kreis T. E. Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin. Cell. 1991 Feb 8;64(3):649–665. doi: 10.1016/0092-8674(91)90248-w. [DOI] [PubMed] [Google Scholar]
  10. Duncan J. R., Kornfeld S. Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus. J Cell Biol. 1988 Mar;106(3):617–628. doi: 10.1083/jcb.106.3.617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Farquhar M. G., Palade G. E. The Golgi apparatus (complex)-(1954-1981)-from artifact to center stage. J Cell Biol. 1981 Dec;91(3 Pt 2):77s–103s. doi: 10.1083/jcb.91.3.77s. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Green S. A., Kelly R. B. Endocytic membrane traffic to the Golgi apparatus in a regulated secretory cell line. J Biol Chem. 1990 Dec 5;265(34):21269–21278. [PubMed] [Google Scholar]
  13. Griffiths G., Fuller S. D., Back R., Hollinshead M., Pfeiffer S., Simons K. The dynamic nature of the Golgi complex. J Cell Biol. 1989 Feb;108(2):277–297. doi: 10.1083/jcb.108.2.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Griffiths G., Pfeiffer S., Simons K., Matlin K. Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J Cell Biol. 1985 Sep;101(3):949–964. doi: 10.1083/jcb.101.3.949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Griffiths G., Rottier P. Cell biology of viruses that assemble along the biosynthetic pathway. Semin Cell Biol. 1992 Oct;3(5):367–381. doi: 10.1016/1043-4682(92)90022-N. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Griffiths G., Simons K. The trans Golgi network: sorting at the exit site of the Golgi complex. Science. 1986 Oct 24;234(4775):438–443. doi: 10.1126/science.2945253. [DOI] [PubMed] [Google Scholar]
  17. Griffiths G., Warren G., Stuhlfauth I., Jockusch B. M. The role of clathrin-coated vesicles in acrosome formation. Eur J Cell Biol. 1981 Dec;26(1):52–60. [PubMed] [Google Scholar]
  18. Hardwick K. G., Boothroyd J. C., Rudner A. D., Pelham H. R. Genes that allow yeast cells to grow in the absence of the HDEL receptor. EMBO J. 1992 Nov;11(11):4187–4195. doi: 10.1002/j.1460-2075.1992.tb05512.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Hauri H. P., Schweizer A. The endoplasmic reticulum-Golgi intermediate compartment. Curr Opin Cell Biol. 1992 Aug;4(4):600–608. doi: 10.1016/0955-0674(92)90078-Q. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Hong W., Tang B. L. Protein trafficking along the exocytotic pathway. Bioessays. 1993 Apr;15(4):231–238. doi: 10.1002/bies.950150403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Hsu V. W., Shah N., Klausner R. D. A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1. Cell. 1992 May 15;69(4):625–635. doi: 10.1016/0092-8674(92)90226-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Hsu V. W., Yuan L. C., Nuchtern J. G., Lippincott-Schwartz J., Hammerling G. J., Klausner R. D. A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecules. Nature. 1991 Aug 1;352(6334):441–444. doi: 10.1038/352441a0. [DOI] [PubMed] [Google Scholar]
  23. Jackson M. R., Nilsson T., Peterson P. A. Retrieval of transmembrane proteins to the endoplasmic reticulum. J Cell Biol. 1993 Apr;121(2):317–333. doi: 10.1083/jcb.121.2.317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Kreis T. E. Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J. 1986 May;5(5):931–941. doi: 10.1002/j.1460-2075.1986.tb04306.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Krijnse-Locker J., Ericsson M., Rottier P. J., Griffiths G. Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. J Cell Biol. 1994 Jan;124(1-2):55–70. doi: 10.1083/jcb.124.1.55. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Lewis M. J., Pelham H. R. A human homologue of the yeast HDEL receptor. Nature. 1990 Nov 8;348(6297):162–163. doi: 10.1038/348162a0. [DOI] [PubMed] [Google Scholar]
  27. Lewis M. J., Pelham H. R. Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell. 1992 Jan 24;68(2):353–364. doi: 10.1016/0092-8674(92)90476-s. [DOI] [PubMed] [Google Scholar]
  28. Lewis M. J., Sweet D. J., Pelham H. R. The ERD2 gene determines the specificity of the luminal ER protein retention system. Cell. 1990 Jun 29;61(7):1359–1363. doi: 10.1016/0092-8674(90)90699-f. [DOI] [PubMed] [Google Scholar]
  29. Lindsey J. D., Ellisman M. H. The neuronal endomembrane system. I. Direct links between rough endoplasmic reticulum and the cis element of the Golgi apparatus. J Neurosci. 1985 Dec;5(12):3111–3123. doi: 10.1523/JNEUROSCI.05-12-03111.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Lindsey J. D., Ellisman M. H. The neuronal endomembrane system. II. The multiple forms of the Golgi apparatus cis element. J Neurosci. 1985 Dec;5(12):3124–3134. doi: 10.1523/JNEUROSCI.05-12-03124.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Lippincott-Schwartz J. Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus. Trends Cell Biol. 1993 Mar;3(3):81–88. doi: 10.1016/0962-8924(93)90078-f. [DOI] [PubMed] [Google Scholar]
  32. Lippincott-Schwartz J., Donaldson J. G., Schweizer A., Berger E. G., Hauri H. P., Yuan L. C., Klausner R. D. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell. 1990 Mar 9;60(5):821–836. doi: 10.1016/0092-8674(90)90096-w. [DOI] [PubMed] [Google Scholar]
  33. Locker J. K., Griffiths G., Horzinek M. C., Rottier P. J. O-glycosylation of the coronavirus M protein. Differential localization of sialyltransferases in N- and O-linked glycosylation. J Biol Chem. 1992 Jul 15;267(20):14094–14101. doi: 10.1016/S0021-9258(19)49683-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Matlin K. S., Simons K. Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell. 1983 Aug;34(1):233–243. doi: 10.1016/0092-8674(83)90154-x. [DOI] [PubMed] [Google Scholar]
  35. Mellman I., Simons K. The Golgi complex: in vitro veritas? Cell. 1992 Mar 6;68(5):829–840. doi: 10.1016/0092-8674(92)90027-A. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Munro S., Pelham H. R. A C-terminal signal prevents secretion of luminal ER proteins. Cell. 1987 Mar 13;48(5):899–907. doi: 10.1016/0092-8674(87)90086-9. [DOI] [PubMed] [Google Scholar]
  37. Neefjes J. J., Verkerk J. M., Broxterman H. J., van der Marel G. A., van Boom J. H., Ploegh H. L. Recycling glycoproteins do not return to the cis-Golgi. J Cell Biol. 1988 Jul;107(1):79–87. doi: 10.1083/jcb.107.1.79. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Oprins A., Duden R., Kreis T. E., Geuze H. J., Slot J. W. Beta-COP localizes mainly to the cis-Golgi side in exocrine pancreas. J Cell Biol. 1993 Apr;121(1):49–59. doi: 10.1083/jcb.121.1.49. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Orci L., Ravazzola M., Meda P., Holcomb C., Moore H. P., Hicke L., Schekman R. Mammalian Sec23p homologue is restricted to the endoplasmic reticulum transitional cytoplasm. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8611–8615. doi: 10.1073/pnas.88.19.8611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Pastan I., Chaudhary V., FitzGerald D. J. Recombinant toxins as novel therapeutic agents. Annu Rev Biochem. 1992;61:331–354. doi: 10.1146/annurev.bi.61.070192.001555. [DOI] [PubMed] [Google Scholar]
  41. Pelham H. R. Control of protein exit from the endoplasmic reticulum. Annu Rev Cell Biol. 1989;5:1–23. doi: 10.1146/annurev.cb.05.110189.000245. [DOI] [PubMed] [Google Scholar]
  42. Pelham H. R. Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 1988 Apr;7(4):913–918. doi: 10.1002/j.1460-2075.1988.tb02896.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Pelham H. R. Recycling of proteins between the endoplasmic reticulum and Golgi complex. Curr Opin Cell Biol. 1991 Aug;3(4):585–591. doi: 10.1016/0955-0674(91)90027-v. [DOI] [PubMed] [Google Scholar]
  44. Pelham H. R. The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem Sci. 1990 Dec;15(12):483–486. doi: 10.1016/0968-0004(90)90303-s. [DOI] [PubMed] [Google Scholar]
  45. Pepperkok R., Scheel J., Horstmann H., Hauri H. P., Griffiths G., Kreis T. E. Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell. 1993 Jul 16;74(1):71–82. doi: 10.1016/0092-8674(93)90295-2. [DOI] [PubMed] [Google Scholar]
  46. Peter F., Nguyen Van P., Söling H. D. Different sorting of Lys-Asp-Glu-Leu proteins in rat liver. J Biol Chem. 1992 May 25;267(15):10631–10637. [PubMed] [Google Scholar]
  47. Peter F., Plutner H., Zhu H., Kreis T. E., Balch W. E. Beta-COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro. J Cell Biol. 1993 Sep;122(6):1155–1167. doi: 10.1083/jcb.122.6.1155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Pind S. N., Nuoffer C., McCaffery J. M., Plutner H., Davidson H. W., Farquhar M. G., Balch W. E. Rab1 and Ca2+ are required for the fusion of carrier vesicles mediating endoplasmic reticulum to Golgi transport. J Cell Biol. 1994 Apr;125(2):239–252. doi: 10.1083/jcb.125.2.239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Roth J., Taatjes D. J., Lucocq J. M., Weinstein J., Paulson J. C. Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell. 1985 Nov;43(1):287–295. doi: 10.1016/0092-8674(85)90034-0. [DOI] [PubMed] [Google Scholar]
  50. Rothman J. E., Orci L. Molecular dissection of the secretory pathway. Nature. 1992 Jan 30;355(6359):409–415. doi: 10.1038/355409a0. [DOI] [PubMed] [Google Scholar]
  51. Rupp K., Birnbach U., Lundström J., Van P. N., Söling H. D. Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase. J Biol Chem. 1994 Jan 28;269(4):2501–2507. [PubMed] [Google Scholar]
  52. Sandvig K., Garred O., Prydz K., Kozlov J. V., Hansen S. H., van Deurs B. Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature. 1992 Aug 6;358(6386):510–512. doi: 10.1038/358510a0. [DOI] [PubMed] [Google Scholar]
  53. Saraste J., Kuismanen E. Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell. 1984 Sep;38(2):535–549. doi: 10.1016/0092-8674(84)90508-7. [DOI] [PubMed] [Google Scholar]
  54. Saraste J., Palade G. E., Farquhar M. G. Antibodies to rat pancreas Golgi subfractions: identification of a 58-kD cis-Golgi protein. J Cell Biol. 1987 Nov;105(5):2021–2029. doi: 10.1083/jcb.105.5.2021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Schekman R. Genetic and biochemical analysis of vesicular traffic in yeast. Curr Opin Cell Biol. 1992 Aug;4(4):587–592. doi: 10.1016/0955-0674(92)90076-o. [DOI] [PubMed] [Google Scholar]
  56. Schmelz M., Sodeik B., Ericsson M., Wolffe E. J., Shida H., Hiller G., Griffiths G. Assembly of vaccinia virus: the second wrapping cisterna is derived from the trans Golgi network. J Virol. 1994 Jan;68(1):130–147. doi: 10.1128/jvi.68.1.130-147.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Schweizer A., Fransen J. A., Bächi T., Ginsel L., Hauri H. P. Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J Cell Biol. 1988 Nov;107(5):1643–1653. doi: 10.1083/jcb.107.5.1643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Schweizer A., Matter K., Ketcham C. M., Hauri H. P. The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi. J Cell Biol. 1991 Apr;113(1):45–54. doi: 10.1083/jcb.113.1.45. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Seetharam S., Chaudhary V. K., FitzGerald D., Pastan I. Increased cytotoxic activity of Pseudomonas exotoxin and two chimeric toxins ending in KDEL. J Biol Chem. 1991 Sep 15;266(26):17376–17381. [PubMed] [Google Scholar]
  60. Semenza J. C., Hardwick K. G., Dean N., Pelham H. R. ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell. 1990 Jun 29;61(7):1349–1357. doi: 10.1016/0092-8674(90)90698-e. [DOI] [PubMed] [Google Scholar]
  61. Singh P., Tang B. L., Wong S. H., Hong W. Transmembrane topology of the mammalian KDEL receptor. Mol Cell Biol. 1993 Oct;13(10):6435–6441. doi: 10.1128/mcb.13.10.6435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Slot J. W., Geuze H. J., Gigengack S., Lienhard G. E., James D. E. Immuno-localization of the insulin regulatable glucose transporter in brown adipose tissue of the rat. J Cell Biol. 1991 Apr;113(1):123–135. doi: 10.1083/jcb.113.1.123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Sodeik B., Doms R. W., Ericsson M., Hiller G., Machamer C. E., van 't Hof W., van Meer G., Moss B., Griffiths G. Assembly of vaccinia virus: role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks. J Cell Biol. 1993 May;121(3):521–541. doi: 10.1083/jcb.121.3.521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Soldati T., Perriard J. C. Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Cell. 1991 Jul 26;66(2):277–289. doi: 10.1016/0092-8674(91)90618-9. [DOI] [PubMed] [Google Scholar]
  65. Sweet D. J., Pelham H. R. The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system. EMBO J. 1992 Feb;11(2):423–432. doi: 10.1002/j.1460-2075.1992.tb05071.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Tang B. L., Wong S. H., Low S. H., Hong W. Retention of a type II surface membrane protein in the endoplasmic reticulum by the Lys-Asp-Glu-Leu sequence. J Biol Chem. 1992 Apr 5;267(10):7072–7076. [PubMed] [Google Scholar]
  67. Tang B. L., Wong S. H., Qi X. L., Low S. H., Hong W. Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor. J Cell Biol. 1993 Jan;120(2):325–338. doi: 10.1083/jcb.120.2.325. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Tang B. L., Wong S. H., Qi X., Subramaniam V. N., Hong W. Golgi-localized beta-galactoside alpha 2,6-sialyltransferase in transfected CHO cells is redistributed into the endoplasmic reticulum by brefeldin A. Eur J Cell Biol. 1992 Oct;59(1):228–231. [PubMed] [Google Scholar]
  69. Tisdale E. J., Bourne J. R., Khosravi-Far R., Der C. J., Balch W. E. GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J Cell Biol. 1992 Nov;119(4):749–761. doi: 10.1083/jcb.119.4.749. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Tooze S. A., Tooze J., Warren G. Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59. J Cell Biol. 1988 May;106(5):1475–1487. doi: 10.1083/jcb.106.5.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Townsley F. M., Wilson D. W., Pelham H. R. Mutational analysis of the human KDEL receptor: distinct structural requirements for Golgi retention, ligand binding and retrograde transport. EMBO J. 1993 Jul;12(7):2821–2829. doi: 10.1002/j.1460-2075.1993.tb05943.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Van P. N., Peter F., Söling H. D. Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles. J Biol Chem. 1989 Oct 15;264(29):17494–17501. [PubMed] [Google Scholar]
  73. Van P. N., Rupp K., Lampen A., Söling H. D. CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity. Eur J Biochem. 1993 Apr 15;213(2):789–795. doi: 10.1111/j.1432-1033.1993.tb17821.x. [DOI] [PubMed] [Google Scholar]
  74. Vaux D., Tooze J., Fuller S. Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal. Nature. 1992 Nov 26;360(6402):372–372. doi: 10.1038/360372a0. [DOI] [PubMed] [Google Scholar]
  75. Weis K., Griffiths G., Lamond A. I. The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif. J Biol Chem. 1994 Jul 22;269(29):19142–19150. [PubMed] [Google Scholar]
  76. Wilson D. W., Lewis M. J., Pelham H. R. pH-dependent binding of KDEL to its receptor in vitro. J Biol Chem. 1993 Apr 5;268(10):7465–7468. [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES