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. 1992 Oct;3(10):1067–1072. doi: 10.1091/mbc.3.10.1067

Endoplasmic reticulum: a dynamic patchwork of specialized subregions.

R Sitia 1, J Meldolesi 1
PMCID: PMC275671  PMID: 1421566

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Selected References

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  1. Arber S., Krause K. H., Caroni P. s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. J Cell Biol. 1992 Jan;116(1):113–125. doi: 10.1083/jcb.116.1.113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bonifacino J. S., Lippincott-Schwartz J. Degradation of proteins within the endoplasmic reticulum. Curr Opin Cell Biol. 1991 Aug;3(4):592–600. doi: 10.1016/0955-0674(91)90028-w. [DOI] [PubMed] [Google Scholar]
  3. Ceriotti A., Colman A. Binding to membrane proteins within the endoplasmic reticulum cannot explain the retention of the glucose-regulated protein GRP78 in Xenopus oocytes. EMBO J. 1988 Mar;7(3):633–638. doi: 10.1002/j.1460-2075.1988.tb02857.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chanat E., Huttner W. B. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J Cell Biol. 1991 Dec;115(6):1505–1519. doi: 10.1083/jcb.115.6.1505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Colley N. J., Baker E. K., Stamnes M. A., Zuker C. S. The cyclophilin homolog ninaA is required in the secretory pathway. Cell. 1991 Oct 18;67(2):255–263. doi: 10.1016/0092-8674(91)90177-z. [DOI] [PubMed] [Google Scholar]
  6. Dabora S. L., Sheetz M. P. The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts. Cell. 1988 Jul 1;54(1):27–35. doi: 10.1016/0092-8674(88)90176-6. [DOI] [PubMed] [Google Scholar]
  7. Ellisman M. H., Deerinck T. J., Ouyang Y., Beck C. F., Tanksley S. J., Walton P. D., Airey J. A., Sutko J. L. Identification and localization of ryanodine binding proteins in the avian central nervous system. Neuron. 1990 Aug;5(2):135–146. doi: 10.1016/0896-6273(90)90304-x. [DOI] [PubMed] [Google Scholar]
  8. Fleischer S., Inui M. Biochemistry and biophysics of excitation-contraction coupling. Annu Rev Biophys Biophys Chem. 1989;18:333–364. doi: 10.1146/annurev.bb.18.060189.002001. [DOI] [PubMed] [Google Scholar]
  9. Fliegel L., Newton E., Burns K., Michalak M. Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum. J Biol Chem. 1990 Sep 15;265(26):15496–15502. [PubMed] [Google Scholar]
  10. Franzini-Armstrong C., Kenney L. J., Varriano-Marston E. The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study. J Cell Biol. 1987 Jul;105(1):49–56. doi: 10.1083/jcb.105.1.49. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Galteau M. M., Antoine B., Reggio H. Epoxide hydrolase is a marker for the smooth endoplasmic reticulum in rat liver. EMBO J. 1985 Nov;4(11):2793–2800. doi: 10.1002/j.1460-2075.1985.tb04005.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gerace L., Burke B. Functional organization of the nuclear envelope. Annu Rev Cell Biol. 1988;4:335–374. doi: 10.1146/annurev.cb.04.110188.002003. [DOI] [PubMed] [Google Scholar]
  13. Gething M. J., Sambrook J. Protein folding in the cell. Nature. 1992 Jan 2;355(6355):33–45. doi: 10.1038/355033a0. [DOI] [PubMed] [Google Scholar]
  14. Haugejorden S. M., Srinivasan M., Green M. Analysis of the retention signals of two resident luminal endoplasmic reticulum proteins by in vitro mutagenesis. J Biol Chem. 1991 Apr 5;266(10):6015–6018. [PubMed] [Google Scholar]
  15. Klausner R. D., Donaldson J. G., Lippincott-Schwartz J. Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol. 1992 Mar;116(5):1071–1080. doi: 10.1083/jcb.116.5.1071. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Klausner R. D., Sitia R. Protein degradation in the endoplasmic reticulum. Cell. 1990 Aug 24;62(4):611–614. doi: 10.1016/0092-8674(90)90104-m. [DOI] [PubMed] [Google Scholar]
  17. Kochevar D. T., Anderson R. G. Purified crystalloid endoplasmic reticulum from UT-1 cells contains multiple proteins in addition to 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem. 1987 Jul 25;262(21):10321–10326. [PubMed] [Google Scholar]
  18. Kreibich G., Sabatini D. D. Sticking together for a difficult passage. Curr Biol. 1992 Feb;2(2):90–92. doi: 10.1016/0960-9822(92)90219-z. [DOI] [PubMed] [Google Scholar]
  19. Lee C., Chen L. B. Dynamic behavior of endoplasmic reticulum in living cells. Cell. 1988 Jul 1;54(1):37–46. doi: 10.1016/0092-8674(88)90177-8. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. 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]
  22. McPherson S. M., McPherson P. S., Mathews L., Campbell K. P., Longo F. J. Cortical localization of a calcium release channel in sea urchin eggs. J Cell Biol. 1992 Mar;116(5):1111–1121. doi: 10.1083/jcb.116.5.1111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Meldolesi J., Madeddu L., Pozzan T. Intracellular Ca2+ storage organelles in non-muscle cells: heterogeneity and functional assignment. Biochim Biophys Acta. 1990 Nov 12;1055(2):130–140. doi: 10.1016/0167-4889(90)90113-r. [DOI] [PubMed] [Google Scholar]
  24. 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]
  25. Michalak M., Milner R. E., Burns K., Opas M. Calreticulin. Biochem J. 1992 Aug 1;285(Pt 3):681–692. doi: 10.1042/bj2850681. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. Newport J. W., Forbes D. J. The nucleus: structure, function, and dynamics. Annu Rev Biochem. 1987;56:535–565. doi: 10.1146/annurev.bi.56.070187.002535. [DOI] [PubMed] [Google Scholar]
  28. Orci L., Brown M. S., Goldstein J. L., Garcia-Segura L. M., Anderson R. G. Increase in membrane cholesterol: a possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells. Cell. 1984 Apr;36(4):835–845. doi: 10.1016/0092-8674(84)90033-3. [DOI] [PubMed] [Google Scholar]
  29. PORTER K. R., PALADE G. E. Studies on the endoplasmic reticulum. III. Its form and distribution in striated muscle cells. J Biophys Biochem Cytol. 1957 Mar 25;3(2):269–300. doi: 10.1083/jcb.3.2.269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Palade G. Intracellular aspects of the process of protein synthesis. Science. 1975 Aug 1;189(4200):347–358. doi: 10.1126/science.1096303. [DOI] [PubMed] [Google Scholar]
  31. Pathak R. K., Luskey K. L., Anderson R. G. Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope. J Cell Biol. 1986 Jun;102(6):2158–2168. doi: 10.1083/jcb.102.6.2158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Pelham H. R. Multiple targets for brefeldin A. Cell. 1991 Nov 1;67(3):449–451. doi: 10.1016/0092-8674(91)90517-3. [DOI] [PubMed] [Google Scholar]
  33. 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]
  34. Petersen O. H., Wakui M. Oscillating intracellular Ca2+ signals evoked by activation of receptors linked to inositol lipid hydrolysis: mechanism of generation. J Membr Biol. 1990 Nov;118(2):93–105. doi: 10.1007/BF01868467. [DOI] [PubMed] [Google Scholar]
  35. Ríos E., Ma J. J., González A. The mechanical hypothesis of excitation-contraction (EC) coupling in skeletal muscle. J Muscle Res Cell Motil. 1991 Apr;12(2):127–135. doi: 10.1007/BF01774031. [DOI] [PubMed] [Google Scholar]
  36. Satoh T., Ross C. A., Villa A., Supattapone S., Pozzan T., Snyder S. H., Meldolesi J. The inositol 1,4,5,-trisphosphate receptor in cerebellar Purkinje cells: quantitative immunogold labeling reveals concentration in an ER subcompartment. J Cell Biol. 1990 Aug;111(2):615–624. doi: 10.1083/jcb.111.2.615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. 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]
  38. Stafford F. J., Bonifacino J. S. A permeabilized cell system identifies the endoplasmic reticulum as a site of protein degradation. J Cell Biol. 1991 Dec;115(5):1225–1236. doi: 10.1083/jcb.115.5.1225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Takei K., Stukenbrok H., Metcalf A., Mignery G. A., Südhof T. C., Volpe P., De Camilli P. Ca2+ stores in Purkinje neurons: endoplasmic reticulum subcompartments demonstrated by the heterogeneous distribution of the InsP3 receptor, Ca(2+)-ATPase, and calsequestrin. J Neurosci. 1992 Feb;12(2):489–505. doi: 10.1523/JNEUROSCI.12-02-00489.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Terasaki M., Jaffe L. A. Organization of the sea urchin egg endoplasmic reticulum and its reorganization at fertilization. J Cell Biol. 1991 Sep;114(5):929–940. doi: 10.1083/jcb.114.5.929. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Thomas K., Navarro J., Benson R. J., Campbell K. P., Rotundo R. L., Fine R. E. Newly synthesized calsequestrin, destined for the sarcoplasmic reticulum, is contained in early/intermediate Golgi-derived clathrin-coated vesicles. J Biol Chem. 1989 Feb 25;264(6):3140–3145. [PubMed] [Google Scholar]
  42. Tooze J., Hollinshead M., Ludwig T., Howell K., Hoflack B., Kern H. In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome. J Cell Biol. 1990 Aug;111(2):329–345. doi: 10.1083/jcb.111.2.329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Tsao Y. S., Ivessa N. E., Adesnik M., Sabatini D. D., Kreibich G. Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process. J Cell Biol. 1992 Jan;116(1):57–67. doi: 10.1083/jcb.116.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. VERATTI E. Investigations on the fine structure of striated muscle fiber read before the Reale Istituto Lombardo, 13 March 1902. J Biophys Biochem Cytol. 1961 Aug;10(4):1–59. doi: 10.1083/jcb.10.4.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Valetti C., Grossi C. E., Milstein C., Sitia R. Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. J Cell Biol. 1991 Nov;115(4):983–994. doi: 10.1083/jcb.115.4.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Villa A., Podini P., Clegg D. O., Pozzan T., Meldolesi J. Intracellular Ca2+ stores in chicken Purkinje neurons: differential distribution of the low affinity-high capacity Ca2+ binding protein, calsequestrin, of Ca2+ ATPase and of the ER lumenal protein, Bip. J Cell Biol. 1991 May;113(4):779–791. doi: 10.1083/jcb.113.4.779. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Villa A., Sharp A. H., Racchetti G., Podini P., Bole D. G., Dunn W. A., Pozzan T., Snyder S. H., Meldolesi J. The endoplasmic reticulum of Purkinje neuron body and dendrites: molecular identity and specializations for Ca2+ transport. Neuroscience. 1992 Jul;49(2):467–477. doi: 10.1016/0306-4522(92)90111-e. [DOI] [PubMed] [Google Scholar]
  48. Volpe P., Villa A., Damiani E., Sharp A. H., Podini P., Snyder S. H., Meldolesi J. Heterogeneity of microsomal Ca2+ stores in chicken Purkinje neurons. EMBO J. 1991 Nov;10(11):3183–3189. doi: 10.1002/j.1460-2075.1991.tb04880.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Volpe P., Villa A., Podini P., Martini A., Nori A., Panzeri M. C., Meldolesi J. The endoplasmic reticulum-sarcoplasmic reticulum connection: distribution of endoplasmic reticulum markers in the sarcoplasmic reticulum of skeletal muscle fibers. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6142–6146. doi: 10.1073/pnas.89.13.6142. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Wallace J. C., Galili G., Kawata E. E., Cuellar R. E., Shotwell M. A., Larkins B. A. Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes. Science. 1988 Apr 29;240(4852):662–664. doi: 10.1126/science.2834822. [DOI] [PubMed] [Google Scholar]
  51. Walter P. Protein translocation. Travelling by TRAM. Nature. 1992 May 7;357(6373):22–23. doi: 10.1038/357022a0. [DOI] [PubMed] [Google Scholar]
  52. Wandelt C. I., Khan M. R., Craig S., Schroeder H. E., Spencer D., Higgins T. J. Vicilin with carboxy-terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants. Plant J. 1992 Mar;2(2):181–192. doi: 10.1046/j.1365-313x.1992.t01-41-00999.x. [DOI] [PubMed] [Google Scholar]
  53. Wikström L., Lodish H. F. Endoplasmic reticulum degradation of a subunit of the asialoglycoprotein receptor in vitro. Vesicular transport from endoplasmic reticulum is unnecessary. J Biol Chem. 1992 Jan 5;267(1):5–8. [PubMed] [Google Scholar]
  54. Yuan S. H., Arnold W., Jorgensen A. O. Biogenesis of transverse tubules and triads: immunolocalization of the 1,4-dihydropyridine receptor, TS28, and the ryanodine receptor in rabbit skeletal muscle developing in situ. J Cell Biol. 1991 Jan;112(2):289–301. doi: 10.1083/jcb.112.2.289. [DOI] [PMC free article] [PubMed] [Google Scholar]

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