» Articles » PMID: 15605178

Identification of a Golgi-localised GRIP Domain Protein from Arabidopsis Thaliana

Overview
Journal Planta
Specialty Biology
Date 2004 Dec 18
PMID 15605178
Citations 9
Authors
Affiliations
Soon will be listed here.
Abstract

A family of Golgi-localised molecules was recently described in animals and fungi possessing extensive coiled regions and a short (approximately 40 residues) conserved C-terminal domain, called the GRIP domain, which is responsible for their location to this organelle. Using the model plant Arabidopsis thaliana, we identified a gene (AtGRIP) encoding a putative GRIP protein. We demonstrated that the C-terminal domain from AtGRIP functions as a Golgi-targeting sequence in plant cells. Localisation studies in living cells expressing the AtGRIP fused to a DsRed2 fluorescent probe, showed extensive co-location with the Golgi marker alpha-mannosidase I in transformed tobacco protoplasts. GRIP-like sequences were also found in genomic databases of rice, maize, wheat and alfalfa, suggesting that this domain may be a useful Golgi marker for immunolocalisation studies. Despite low sequence identity amongst GRIP domains, the plant GRIP sequence was able to target to the Golgi of mammalian cells. Taken together, these data indicate that GRIP domain proteins might be implicated in a targeting mechanism that is conserved amongst eukaryotes.

Citing Articles

A sophisticated, differentiated Golgi in the ancestor of eukaryotes.

Barlow L, Nyvltova E, Aguilar M, Tachezy J, Dacks J BMC Biol. 2018; 16(1):27.

PMID: 29510703 PMC: 5840792. DOI: 10.1186/s12915-018-0492-9.


Stacks off tracks: a role for the golgin AtCASP in plant endoplasmic reticulum-Golgi apparatus tethering.

Osterrieder A, Sparkes I, Botchway S, Ward A, Ketelaar T, de Ruijter N J Exp Bot. 2017; 68(13):3339-3350.

PMID: 28605454 PMC: 5853478. DOI: 10.1093/jxb/erx167.


The C-TERMINUS of AtGRIP is crucial for its self-association and for targeting to Golgi stacks in Arabidopsis.

Zhao L, Li Y PLoS One. 2014; 9(6):e98963.

PMID: 24901770 PMC: 4047078. DOI: 10.1371/journal.pone.0098963.


Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185.

Burguete A, Fenn T, Brunger A, Pfeffer S Cell. 2008; 132(2):286-98.

PMID: 18243103 PMC: 2344137. DOI: 10.1016/j.cell.2007.11.048.


A red fluorescent protein, DsRed2, as a visual reporter for transient expression and stable transformation in soybean.

Nishizawa K, Kita Y, Kitayama M, Ishimoto M Plant Cell Rep. 2006; 25(12):1355-61.

PMID: 16841215 DOI: 10.1007/s00299-006-0210-x.


References
1.
Munro S, Nichols B . The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins. Curr Biol. 1999; 9(7):377-80. DOI: 10.1016/s0960-9822(99)80166-3. View

2.
Gish W, States D . Identification of protein coding regions by database similarity search. Nat Genet. 1993; 3(3):266-72. DOI: 10.1038/ng0393-266. View

3.
Gleeson P, Anderson T, Stow J, Griffiths G, Toh B, MATHESON F . p230 is associated with vesicles budding from the trans-Golgi network. J Cell Sci. 1996; 109 ( Pt 12):2811-21. DOI: 10.1242/jcs.109.12.2811. View

4.
McConville M, Ilgoutz S, Teasdale R, Foth B, Matthews A, Mullin K . Targeting of the GRIP domain to the trans-Golgi network is conserved from protists to animals. Eur J Cell Biol. 2002; 81(9):485-95. DOI: 10.1078/0171-9335-00268. View

5.
Kjer-Nielsen L, Teasdale R, van Vliet C, Gleeson P . A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr Biol. 1999; 9(7):385-8. DOI: 10.1016/s0960-9822(99)80168-7. View