Journal of Cell Science, Vol 103, Issue 3 773-784, Copyright © 1992 by Company of Biologists

JOURNAL ARTICLES

Adhesion of Golgi cisternae by proteinaceous interactions: intercisternal bridges as putative adhesive structures

EB Cluett and WJ Brown
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.

We have investigated the nature of the component(s) responsible for holding the cisternal membranes of the Golgi complex into a stacked unit. Isolated Golgi complexes were treated with a variety of agents to induce the separation of intact Golgi stacks into single cisternal elements, i.e. "unstacking", and the effects were analyzed and quantitated by electron microscopy. In control experiments, isolated, intact Golgi stacks were stable at 4 degrees C and 20 degrees C for > or = 1 h; however, some unstacking occurred at 32 degrees C. Treatment of intact Golgi stacks with a variety of proteolytic enzymes resulted in a time- and dose-dependent unstacking of the cisternae, although stacks were resistant to various other proteases. Following liberation from the stack, single cisternae remained flattened with dilated rims. The integrity of intact Golgi stacks was unaffected by treatment with various concentrations and combinations of monovalent and divalent cations, or chelators of divalent cations. Electron microscopic observations of tannic acid- or negatively stained Golgi complexes, revealed the presence of highly structured, intercisternal "bridges". When seen within intact Golgi complexes, these bridges were only consistently found between closely apposed cisternae and were not observed on dilated rims or secretory vesicles. These bridges, on both intact stacks and physically disrupted cisternae, were rectangular, being approximately 8.5 nm in width, approximately 11 nm in height. Treatment with proteases under conditions that resulted in the with proteases under conditions that resulted in the unstacking of intact complexes also removed these bridge structures. These data show that proteinaceous components are responsible for holding Golgi cisternae together into a cohesive, stacked unit, and identify a candidate bridge structure that could serve this purpose.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				S.-i. Yoshimura, A. Yamamoto, Y. Misumi, M. Sohda, F. A. Barr, G. Fujii, A. Shakoori, H. Ohno, K. Mihara, and N. Nakamura Dynamics of Golgi Matrix Proteins after the Blockage of ER to Golgi Transport J. Biochem., February 1, 2004; 135(2): 201 - 216. [Abstract] [Full Text] [PDF]

				E. L. Snapp, R. S. Hegde, M. Francolini, F. Lombardo, S. Colombo, E. Pedrazzini, N. Borgese, and J. Lippincott-Schwartz Formation of stacked ER cisternae by low affinity protein interactions J. Cell Biol., October 27, 2003; 163(2): 257 - 269. [Abstract] [Full Text] [PDF]

				A. CARAFA, J. G. DUCKETT, and R. LIGRONE The Placenta in Monoclea forsteri Hook. and Treubia lacunosa (Col.) Prosk: Insights into Placental Evolution in Liverworts Ann. Bot., August 1, 2003; 92(2): 299 - 307. [Abstract] [Full Text] [PDF]

				D. Drecktrah, K. Chambers, E. L. Racoosin, E. B. Cluett, A. Gucwa, B. Jackson, and W. J. Brown Inhibition of a Golgi Complex Lysophospholipid Acyltransferase Induces Membrane Tubule Formation and Retrograde Trafficking Mol. Biol. Cell, August 1, 2003; 14(8): 3459 - 3469. [Abstract] [Full Text] [PDF]

				J. D. Lane, J. Lucocq, J. Pryde, F. A. Barr, P. G. Woodman, V. J. Allan, and M. Lowe Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis J. Cell Biol., February 4, 2002; 156(3): 495 - 509. [Abstract] [Full Text] [PDF]

				P. de Figueiredo, R. S. Polizotto, D. Drecktrah, and W. J. Brown Membrane Tubule-mediated Reassembly and Maintenance of the Golgi Complex Is Disrupted by Phospholipase A2 Antagonists Mol. Biol. Cell, June 1, 1999; 10(6): 1763 - 1782. [Abstract] [Full Text]

				O. W. Rossanese, J. Soderholm, B. J. Bevis, I. B. Sears, J. O'Connor, E. K. Williamson, and B. S. Glick Golgi Structure Correlates with Transitional Endoplasmic Reticulum Organization in Pichia pastoris and Saccharomyces cerevisiae J. Cell Biol., April 5, 1999; 145(1): 69 - 81. [Abstract] [Full Text] [PDF]

				L. Orci, A. Perrelet, and J. E. Rothman Vesicles on strings: Morphological evidence for processive transport within the Golgi stack PNAS, March 3, 1998; 95(5): 2279 - 2283. [Abstract] [Full Text] [PDF]

				D Drecktrah, P de Figueiredo, R. Mason, and W. Brown Retrograde trafficking of both Golgi complex and TGN markers to the ER induced by nordihydroguaiaretic acid and cyclofenil diphenol J. Cell Sci., January 4, 1998; 111(7): 951 - 965. [Abstract] [PDF]

				A. Mironov, A. Colanzi, M. G. Silletta, G. Fiucci, S. Flati, A. Fusella, R. Polishchuk, A. Mironov Jr., G. D. Tullio, R. Weigert, et al. Role of NAD+ and ADP-Ribosylation in the Maintenance of the Golgi Structure J. Cell Biol., December 1, 1997; 139(5): 1109 - 1118. [Abstract] [Full Text] [PDF]

				E. B. Cluett, E. Kuismanen, and C. E. Machamer Heterogeneous Distribution of the Unusual Phospholipid Semilysobisphosphatidic Acid through the Golgi Complex Mol. Biol. Cell, November 1, 1997; 8(11): 2233 - 2240. [Abstract] [Full Text]

				A. A. Mironov, P. Weidman, and A. Luini Variations on the Intracellular Transport Theme: Maturing Cisternae and Trafficking Tubules J. Cell Biol., August 11, 1997; 138(3): 481 - 484. [Full Text] [PDF]

				E. Cluett and C. Machamer The envelope of vaccinia virus reveals an unusual phospholipid in Golgi complex membranes J. Cell Sci., January 8, 1996; 109(8): 2121 - 2131. [Abstract] [PDF]

				J. Pryde A group of integral membrane proteins of the rat liver Golgi contains a conserved protein of 100 kDa J. Cell Sci., January 12, 1994; 107(12): 3425 - 3436. [Abstract] [PDF]

				K Ayscough, N. Hajibagheri, R Watson, and G Warren Stacking of Golgi cisternae in Schizosaccharomyces pombe requires intact microtubules J. Cell Sci., January 12, 1993; 106(4): 1227 - 1237. [Abstract] [PDF]

				C.-Y. Lin, M. L. Madsen, F. R. Yarm, Y.-J. Jang, X. Liu, and R. L. Erikson Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2 PNAS, November 7, 2000; 97(23): 12589 - 12594. [Abstract] [Full Text] [PDF]

				J. D. Lane, J. Lucocq, J. Pryde, F. A. Barr, P. G. Woodman, V. J. Allan, and M. Lowe Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis J. Cell Biol., February 4, 2002; 156(3): 495 - 509. [Abstract] [Full Text] [PDF]