QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 2 November 2004
doi: 10.1242/jcs.01497

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.01497v1 117/24/5865    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Derby, M. C. Articles by Gleeson, P. A. Search for Related Content PubMed PubMed Citation Articles by Derby, M. C. Articles by Gleeson, P. A.

Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN

¹ The Russell Grimwade School of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Victoria 3010, Australia
² Institute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia
³ School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia
⁴ Laboratory of Membrane Biology, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Rep. of Singapore

^* Author for correspondence (e-mail: pgleeson{at}unimelb.edu.au)

Accepted 17 August 2004

The four mammalian golgins, p230/golgin-245, golgin-97, GCC88 and GCC185 are targeted to trans-Golgi network (TGN) membranes by their C-terminal GRIP domain in a G-protein-dependent process. The Arf-like GTPase, Arl1, has been shown to mediate TGN recruitment of p230/golgin245 and golgin-97 by interaction with their GRIP domains; however, it is not known whether all the TGN golgins bind to Arl1 and whether they are all recruited to the same or different TGN domains. Here we demonstrate differences in membrane binding properties and TGN domain recruitment of the mammalian GRIP domain proteins. Overexpression of full-length GCC185 resulted in the appearance of small punctate structures dispersed in the cytoplasm of transfected cells that were identified as membrane tubular structures by immunoelectron microscopy. The cytoplasmic GCC185-labelled structures were enriched for membrane binding determinants of GCC185 GRIP, whereas the three other mammalian GRIP family members did not colocalize with the GCC185-labelled structures. These GCC185-labelled structures included the TGN resident protein 2,6 sialyltransferase and excluded the recycling TGN protein, TGN46. The Golgi stack was unaffected by overexpression of GCC185. Overexpression of both full-length GCC185 and GCC88 showed distinct and nonoverlapping structures. We also show that the GRIP domains of GCC185 and GCC88 differ in membrane binding properties from each other and, in contrast to p230/golgin-245 and golgin-97, do not interact with Arl1 in vivo. Collectively these results show that GCC88, GCC185 and p230/golgin245 are recruited to functionally distinct domains of the TGN and are likely to be important for the maintenance of TGN subdomain structure, a critical feature for mediating protein sorting and membrane transport.

Key words: Golgins, GRIP domain, Tethers, trans-Golgi network, Arl1

This article has been cited by other articles:

				G. L. Hayes, F. C. Brown, A. K. Haas, R. M. Nottingham, F. A. Barr, and S. R. Pfeffer Multiple Rab GTPase Binding Sites in GCC185 Suggest a Model for Vesicle Tethering at the Trans-Golgi Mol. Biol. Cell, January 1, 2009; 20(1): 209 - 217. [Abstract] [Full Text] [PDF]

				C. J. Guerriero, Y. Lai, and O. A. Weisz Differential Sorting and Golgi Export Requirements for Raft-associated and Raft-independent Apical Proteins along the Biosynthetic Pathway J. Biol. Chem., June 27, 2008; 283(26): 18040 - 18047. [Abstract] [Full Text] [PDF]

				Z. G. Holloway, R. Grabski, T. Szul, M. L. Styers, J. A. Coventry, A. P. Monaco, and E. Sztul Activation of ADP-ribosylation factor regulates biogenesis of the ATP7A-containing trans-Golgi network compartment and its Cu-induced trafficking Am J Physiol Cell Physiol, December 1, 2007; 293(6): C1753 - C1767. [Abstract] [Full Text] [PDF]

				Z. Z. Lieu, M. C. Derby, R. D. Teasdale, C. Hart, P. Gunn, and P. A. Gleeson The Golgin GCC88 Is Required for Efficient Retrograde Transport of Cargo from the Early Endosomes to the Trans-Golgi Network Mol. Biol. Cell, December 1, 2007; 18(12): 4979 - 4991. [Abstract] [Full Text] [PDF]

				T. Szul, R. Grabski, S. Lyons, Y. Morohashi, S. Shestopal, M. Lowe, and E. Sztul Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking J. Cell Sci., November 15, 2007; 120(22): 3929 - 3940. [Abstract] [Full Text] [PDF]

				J. V. Reddy, A. S. Burguete, K. Sridevi, I. G. Ganley, R. M. Nottingham, and S. R. Pfeffer A Functional Role for the GCC185 Golgin in Mannose 6-Phosphate Receptor Recycling Mol. Biol. Cell, October 1, 2006; 17(10): 4353 - 4363. [Abstract] [Full Text] [PDF]

				E. Sztul and V. Lupashin Role of tethering factors in secretory membrane traffic Am J Physiol Cell Physiol, January 1, 2006; 290(1): C11 - C26. [Abstract] [Full Text] [PDF]

				C. M. Snyder, G. A. Mardones, M. S. Ladinsky, and K. E. Howell GMx33 Associates with the Trans-Golgi Matrix in a Dynamic Manner and Sorts within Tubules Exiting the Golgi Mol. Biol. Cell, January 1, 2006; 17(1): 511 - 524. [Abstract] [Full Text] [PDF]

				A. Yoshino, S. R. G. Setty, C. Poynton, E. L. Whiteman, A. Saint-Pol, C. G. Burd, L. Johannes, E. L. Holzbaur, M. Koval, J. M. McCaffery, et al. tGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre J. Cell Sci., May 15, 2005; 118(10): 2279 - 2293. [Abstract] [Full Text] [PDF]