Identification of a Golgi-localised GRIP domain protein from Arabidopsis thaliana

Gilson, Paul R.; Vergara, Claudia E.; Teasdale, Rohan D.; Bacic, Antony; Gleeson, Paul A.

doi:10.1007/s00425-004-1311-9

Cited by 34 publications

(45 citation statements)

References 30 publications

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“…The spectral properties of mGFP5 allow efficient spectral separation from YFP (Brandizzi et al, 2002). The coding sequence of GRIP (amino acids 578-788 of the peripheral Golgi matrix protein AtGRIP (Gilson et al, 2004), Genebank accession number: AF370325) was a generous gift of Dr P. Gleeson, University of Melbourne, Australia, and it was amplified with primers containing the BamHI and SacI sites for subcloning downstream of YFP in the binary vector pVKH18-En6 (Batoko et al, 2000). cDNA of ARL1 (At2g24765) was obtained as an ABRC clone and fused to the N-terminus of a YFP using the XbaI and SalI sites of the binary vector pVKH18-En6.…”

Section: Molecular Cloningmentioning

confidence: 99%

“…The Arabidopsis genome encodes homologues of mammalian and yeast peripheral golgins (Gillingham et al, 2002;Rose et al, 2004), and the Golgi localization of a green fluorescent protein fusion to the GRIP domain of a peripheral Arabidopsis golgin (At-GRIP) and of the full-length AtGRIP has been reported (Gilson et al, 2004;Latijnhouwers et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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ARL1 Plays a Role in the Binding of the GRIP Domain of a Peripheral Matrix Protein to the Golgi Apparatus in Plant Cells

et al. 2006

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ARF GTPases play a central role in regulating membrane dynamics and protein transport in eukaryotic cells. ARF-like (ARL) proteins are close relatives of the ARF regulators of vesicular transport, but their function in plant cells is poorly characterized. Here, by means of live cell imaging and site-directed mutagenesis, we have investigated the cellular function of the plant GTPase ARL1. We provide direct evidence for a role of this ARL family member in the association of a plant golgin with the plant Golgi apparatus. Our data reveal the existence of key residues within the conserved GRIP-domain of the golgin and within the GTPase ARL1 that are central to ARL1-GRIP interaction. Mutations of these residues abolish the interaction of GRIP with the GTP-bound ARL1 and induce a redistribution of GRIP into the cytosol. This indicates that the localization of GRIP to the Golgi apparatus is strongly influenced by the interaction of GRIP with Golgi-localized ARL1. Our results assign a cellular role to a member of the Arabidopsis ARL family in the plant secretory pathway and propose mechanisms for localization of peripheral golgins to the plant Golgi apparatus.

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Section: Molecular Cloningmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

ARL1 Plays a Role in the Binding of the GRIP Domain of a Peripheral Matrix Protein to the Golgi Apparatus in Plant Cells

et al. 2006

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“…The importance of TGN golgins is highlighted by the finding that GRIP domain proteins are conserved throughout evolution, as functional GRIP targeting sequences have been identified in yeast, plants and protozoan parasites (Munro and Nichols, 1999;McConville et al, 2002;Gilson et al, 2004). Given the molecular characteristics of the GRIP domain family it is likely that they play a role similar to the golgins of the Golgi stack, as either matrix components and/or in vesicular tethering .…”

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confidence: 99%

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

Derby

Vliet

Brown

et al. 2004

Journal of Cell Science

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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 α2,6 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.

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“…Although a few homologues of Golgins can be found in the arabidopsis genome, to date no information exists as to their function. Recently, an arabidopsis gene AtGRIP1, which encodes for a putative GRIP protein has been shown to target the plant Golgi (Gilson et al, 2004). Rab6, involved in retrograde transport in the mammalian Golgi stack (Sannerud et al, 2003), is thought to mediate vesicle tethering and also binds GRIP domains and the dynactin complex.…”

Section: Holding It All Togethermentioning

confidence: 99%

Cell biology of the plant Golgi apparatus

Hawes

2004

New Phytologist

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The higher plant Golgi apparatus, comprising many individual stacks of membrane bounded cisternae, is one of the most enigmatic of the cytoplasmic organelles. Not only can the stacks receive material from the endoplasmic reticulum, process it and target it to the correct cellular destination, but they can also synthesise and export complex carbohydrates and lipids and most likely act as one end point of the endocytic pathway. In many cells such processing and sorting can take place while the stacks are moving within the cytoplasm and, remarkably, the organelle manages to retain its structural integrity. This review considers some of the latest data and views on transport both to and from the Golgi and the mechanisms by which such activity is regulated.

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Identification of a Golgi-localised GRIP domain protein from Arabidopsis thaliana

Cited by 34 publications

References 30 publications

ARL1 Plays a Role in the Binding of the GRIP Domain of a Peripheral Matrix Protein to the Golgi Apparatus in Plant Cells

ARL1 Plays a Role in the Binding of the GRIP Domain of a Peripheral Matrix Protein to the Golgi Apparatus in Plant Cells

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

Cell biology of the plant Golgi apparatus

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