Effect of Caffeine and Reduced Temperature (20 Degrees C) on the Organization of the Pre-Golgi and the Golgi Stack Membranes

Overview

Journal J Cell Biol

Specialty Cell Biology

Date 1993 Mar 1

PMID 8449979

Citations 6

Authors

J Jantti

E Kuismanen

Affiliations

Soon will be listed here.

Abstract

In the present study we have dissected the transport pathways between the ER and the Golgi complex using a recently introduced (Kuismanen, E., J. Jäntti, V. Mäkiranta, and M. Sariola. 1992. J. Cell Sci. 102:505-513) inhibition of transport by caffeine at 20 degrees C. Recovery of the Golgi complex from brefeldin A (BFA) treatment was inhibited by caffeine at reduced temperature (20 degrees C) suggesting that caffeine inhibits the membrane traffic between the ER and the Golgi complex. Caffeine at 20 degrees C did not inhibit the BFA-induced retrograde movement of the Golgi membranes. Further, incubation of the cells in 10 mM caffeine at 20 degrees C had profound effects on the distribution and the organization of the pre-Golgi and the Golgi stack membranes. Caffeine treatment at 20 degrees C resulted in a selective and reversible translocation of the pre- and cis-Golgi marker protein (p58) to the periphery of the cell. This caffeine-induced effect on the Golgi complex was different from that induced by BFA, since mannosidase II, a Golgi stack marker, remained perinuclearly located and the Golgi stack coat protein, beta-COP, was not detached from Golgi membranes in the presence of 10 mM caffeine at 20 degrees C. Electron microscopic analysis showed that, in the presence of caffeine at 20 degrees C, the morphology of the Golgi stack was altered and accumulation of numerous small vesicles in the Golgi region was observed. The results in the present study suggest that caffeine at reduced temperature (20 degrees C) reveals a functional interface between the pre-Golgi and the Golgi stack.

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References

Downes C, Musk S, Watson J, Johnson R . Caffeine overcomes a restriction point associated with DNA replication, but does not accelerate mitosis. J Cell Biol. 1990; 110(6):1855-9. PMC: 2116112. DOI: 10.1083/jcb.110.6.1855. View

Balch W, Dunphy W, Braell W, Rothman J . Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell. 1984; 39(2 Pt 1):405-16. DOI: 10.1016/0092-8674(84)90019-9. View

Kuismanen E, Saraste J . Low temperature-induced transport blocks as tools to manipulate membrane traffic. Methods Cell Biol. 1989; 32:257-74. DOI: 10.1016/s0091-679x(08)61174-7. View

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

Klausner R, Donaldson J, Lippincott-Schwartz J . Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol. 1992; 116(5):1071-80. PMC: 2289364. DOI: 10.1083/jcb.116.5.1071. View

Barr F, Leyte A, Mollner S, Pfeuffer T, Tooze S, Huttner W . Trimeric G-proteins of the trans-Golgi network are involved in the formation of constitutive secretory vesicles and immature secretory granules. FEBS Lett. 1991; 294(3):239-43. DOI: 10.1016/0014-5793(91)81438-e. View

Chavrier P, Parton R, Hauri H, Simons K, Zerial M . Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell. 1990; 62(2):317-29. DOI: 10.1016/0092-8674(90)90369-p. View

Duden R, Griffiths G, Frank R, Argos P, Kreis T . Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin. Cell. 1991; 64(3):649-65. DOI: 10.1016/0092-8674(91)90248-w. View

Beckers C, Balch W . Calcium and GTP: essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus. J Cell Biol. 1989; 108(4):1245-56. PMC: 2115521. DOI: 10.1083/jcb.108.4.1245. View

10.

Machamer C, Mentone S, Rose J, Farquhar M . The E1 glycoprotein of an avian coronavirus is targeted to the cis Golgi complex. Proc Natl Acad Sci U S A. 1990; 87(18):6944-8. PMC: 54658. DOI: 10.1073/pnas.87.18.6944. View

11.

Saraste J, Kuismanen E . Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex. Semin Cell Biol. 1992; 3(5):343-55. PMC: 7128811. DOI: 10.1016/1043-4682(92)90020-v. View

12.

Matlin K, Skibbens J, McNeil P . Reduced extracellular pH reversibly inhibits oligomerization, intracellular transport, and processing of the influenza hemagglutinin in infected Madin-Darby canine kidney cells. J Biol Chem. 1988; 263(23):11478-85. View

13.

Saraste J, von Bonsdorff C, Hashimoto K, Kaariainen L, Keranen S . Semliki forest virus mutants with temperature-sensitive transport defect of envelope proteins. Virology. 1980; 100(2):229-45. DOI: 10.1016/0042-6822(80)90516-4. View

14.

Rothman J, Orci L . Molecular dissection of the secretory pathway. Nature. 1992; 355(6359):409-15. DOI: 10.1038/355409a0. View

15.

Brown W, Farquhar M . Immunoperoxidase methods for the localization of antigens in cultured cells and tissue sections by electron microscopy. Methods Cell Biol. 1989; 31:553-69. DOI: 10.1016/s0091-679x(08)61626-x. View

16.

Plutner H, Cox A, Pind S, Khosravi-Far R, Bourne J, Schwaninger R . Rab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. J Cell Biol. 1991; 115(1):31-43. PMC: 2289927. DOI: 10.1083/jcb.115.1.31. View

17.

Lewis M, Pelham H . A human homologue of the yeast HDEL receptor. Nature. 1990; 348(6297):162-3. DOI: 10.1038/348162a0. View

18.

Davidson H, McGowan C, Balch W . Evidence for the regulation of exocytic transport by protein phosphorylation. J Cell Biol. 1992; 116(6):1343-55. PMC: 2289369. DOI: 10.1083/jcb.116.6.1343. View

19.

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; 38(2):535-49. DOI: 10.1016/0092-8674(84)90508-7. View

20.

Lodish H, Kong N . Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J Biol Chem. 1990; 265(19):10893-9. View