Abstract
Golgi complex beads are 10-nm particles arranged in rings on the smooth surface of rough endoplasmic reticulum (ER) makind the forming face of the Golgi complex (GC). In arthropod cells they stain specifically with bismuth. Their morphology has been studied after treatment with reagents known to interfere with GC function. Inhibitors of oxidative phosphorylation (antimycin A, cyanide, and anoxia), but not an inhibitor of glycolysis (iodoacetate), both cause the bead rings to collapse and the GC saccules to round up, and inhibit transition vesicle (TV) formation. Cycloheximide blocks protein synthesis on ribosomes but does not stop TV formation or disrupt bead rings, even after prolonged treatment (6 h) to allow emptying of the rough ER cisternae. Thus the collapse of bead rings is not attributable to inhibition of protein synthesis, and the ring structure of beads does not require continued protein synthesis and secretion for its maintenance. Valinomycin has effects on the GC similar to those of antimycin A, but A23187, monensin, and lasalocid do not affect bead ring structure or TV formation. These results are consistent with valinomycin’s secondarily uncoupling mitochondria, which collapses bead rings and prevents TV formation. Thus inhibitors of oxidative phosphorylation do not influence the beads through cation movement. Because mononsin and lasalocid block secretion at the level of the condensing vacuoles, bead rings are not influenced by blocks in secretion distal to them or by the backup of secretory material. These experiments are consistent with inhibitors of oxidative phosphorylation collapsing bead rings by decreasing intracellular ATP. The concomitant block to TV formation and the collapse of bead rings suggests that integrity of the bead rings is essential for the transport of secretory material from the rough ER to the GC.
Full Text
The Full Text of this article is available as a PDF (1.3 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Chandler D. E., Williams J. A. Intracellular divalent cation release in pancreatic acinar cells during stimulus-secretion coupling. II. Subcellular localization of the fluorescent probe chlorotetracycline. J Cell Biol. 1978 Feb;76(2):386–399. doi: 10.1083/jcb.76.2.386. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J Cell Biol. 1967 Aug;34(2):577–596. doi: 10.1083/jcb.34.2.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. IV. Metabolic requirements. J Cell Biol. 1968 Dec;39(3):589–603. doi: 10.1083/jcb.39.3.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Locke M., Collins J. V. Protein uptake into multivesicular bodies and storage granules in the fat body of an insect. J Cell Biol. 1968 Mar;36(3):453–483. doi: 10.1083/jcb.36.3.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Locke M., Huie P. Bismuth staining for light and electron microscopy. Tissue Cell. 1977;9(2):347–371. doi: 10.1016/0040-8166(77)90026-x. [DOI] [PubMed] [Google Scholar]
- Locke M., Huie P. Golgi complex--endoplasmic reticulum transition region has rings of beads. Science. 1975 Jun 20;188(4194):1219–1221. doi: 10.1126/science.49926. [DOI] [PubMed] [Google Scholar]
- Locke M., Huie P. The beads in the Golgi complex-endoplasmic reticulum region. J Cell Biol. 1976 Aug;70(2 Pt 1):384–394. doi: 10.1083/jcb.70.2.384. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Locke M., Huie P. Vertebrate Golgi complexes have beads in a similar position to those found in arthropods. Tissue Cell. 1976;8(4):739–743. doi: 10.1016/0040-8166(76)90043-4. [DOI] [PubMed] [Google Scholar]
- Pressman B. C. Biological applications of ionophores. Annu Rev Biochem. 1976;45:501–530. doi: 10.1146/annurev.bi.45.070176.002441. [DOI] [PubMed] [Google Scholar]
- Reed P. W. Ionophores. Methods Enzymol. 1979;55:435–454. doi: 10.1016/0076-6879(79)55058-7. [DOI] [PubMed] [Google Scholar]
- Rottenberg H. ATP synthesis and electrical membrane potential in mitochondria. Eur J Biochem. 1970 Jul;15(1):22–28. doi: 10.1111/j.1432-1033.1970.tb00971.x. [DOI] [PubMed] [Google Scholar]
- Rottenberg H., Scarpa A. Calcium uptake and membrane potential in mitochondria. Biochemistry. 1974 Nov 5;13(23):4811–4817. doi: 10.1021/bi00720a020. [DOI] [PubMed] [Google Scholar]
- Somlyo A. P., Garfield R. E., Chacko S., Somlyo A. V. Golgi organelle response to the antibiotic X537A. J Cell Biol. 1975 Aug;66(2):425–443. doi: 10.1083/jcb.66.2.425. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tartakoff A., Vassalli P., Détraz M. Comparative studies of intracellular transport of secretory proteins. J Cell Biol. 1978 Dec;79(3):694–707. doi: 10.1083/jcb.79.3.694. [DOI] [PMC free article] [PubMed] [Google Scholar]