Targeting of the GRIP domain to the trans-Golgi network is conserved from protists to animals

McConville, M. J., Ilgoutz, S. C., Teasdale, R. D., Foth, B. J., Matthews, A., Mullin, K. A. and Gleeson, P A. (2002) Targeting of the GRIP domain to the trans-Golgi network is conserved from protists to animals. European Journal of Cell Biology, 81 9: 485-495. doi:10.1078/0171-9335-00268

Author McConville, M. J.
Ilgoutz, S. C.
Teasdale, R. D.
Foth, B. J.
Matthews, A.
Mullin, K. A.
Gleeson, P A.
Title Targeting of the GRIP domain to the trans-Golgi network is conserved from protists to animals
Journal name European Journal of Cell Biology   Check publisher's open access policy
ISSN 0171-9335
Publication date 2002-01-01
Year available 2002
Sub-type Article (original research)
DOI 10.1078/0171-9335-00268
Open Access Status Not yet assessed
Volume 81
Issue 9
Start page 485
End page 495
Total pages 11
Place of publication Jena
Publisher Urban & Fischer Verlag
Language eng
Subject 2734 Pathology and Forensic Medicine
2722 Histology
1307 Cell Biology
Abstract The GRIP domain, found in a family of coiled-coil peripheral membrane Golgi proteins, is a specific targeting sequence for the trans-Golgi network of animal cells. In this study we show that a coiled-coil protein with a GRIP domain occurs in the primitive eukaryote, Trypanosoma brucei, and that reporter proteins containing this domain can be used as a marker for the poorly characterized trans Golgi/trans-Golgi network of trypanosomatid parasites. The T brucei GRIP domain, when fused to the carboxyl terminus of the green fluorescent protein (GFP-Tb-GRIP), was efficiently localized to the Golgi apparatus of transfected COS cells. Overexpression of GFP-TbGRIP in COS cells displaced the endogenous GRIP protein, GCC1p, from the Golgi apparatus indicating that the trypanosomatid and mammalian GRIP sequences interact with similar membrane determinants. GFP fusion proteins containing either the T brucei GRIP domain or the human p230 GRIP (p230(GRIP)) domain were also expressed in the trypanosomatid parasite, Leishmania mexicana, and localized by fluorescence and immuno-electron microscopy to the trans face of the single Golgi apparatus and a short tubule that extended from the Golgi apparatus. Binding of GFP-p230(GRIP) to Golgi membranes in L. mexicana was abrogated by mutation of a critical tyrosine residue in the p230 GRIP domain. The levels of GFP-GRIP fusion proteins were dramatically reduced in stationary-phase L. mexicana promastigotes, suggesting that specific Golgi trafficking steps may be down-regulated as the promastigotes cease dividing. This study provides a protein marker for the trans-Golgi network of trypanosomatid parasites and suggests that the GRIP domain binds to a membrane component that has been highly conserved in eukaryotic evolution.
Keyword Cell Biology
GRIP domain
trans-Golgi network
vesicular transport
Leishmania mexicana
Trypanosoma brucei
Oxysterol-binding Protein
Coiled-coil Proteins
Px Domains
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 37 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 20 Sep 2007, 01:44:29 EST