PRA Isoforms Are Targeted to Distinct Membrane Compartments

Abdul‐Ghani, Mohammad; Gougeon, Pierre‐Yves; Prosser, Derek C.; DaSilva, Lance F; Ngsee, Johnny K.

doi:10.1074/jbc.m009073200

Cited by 74 publications

(92 citation statements)

References 45 publications

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“…Regarding the spatial distribution, PRA1 homologs have been ubiquitously found in human tissues, emphasizing their importance for development (Martincic et al, 1997;Abdul-Ghani et al, 2001;Bucci et al, 2001;Schweneker et al, 2005;Fo et al, 2006). Based on our results in 8-d-old seedlings, AtPRA1 transcripts are differently distributed, mainly accumulating in emerging organs and vascular tissues.…”

Section: Discussionmentioning

confidence: 87%

“…In human, yeast, and mouse, PRA1 resides predominantly in the Golgi apparatus (Liang and Li, 2000;Huh et al, 2003;Sivars et al, 2003). However, PRA1 proteins have been reported in different trafficking compartments, such as the ER (Abdul-Ghani et al, 2001;Schweneker et al, 2005;Liu et al, 2006), synaptic vesicles (Fenster et al, 2000), COPI and COPII vesicles (Otte et al, 2001;Gilchrist et al, 2006), and endosomes (Schweneker et al, 2005;Geerts et al, 2007). To determine the subcellular localization of the 19 AtPRA1 proteins, their full-length open reading frames were fused to the enhanced GFP reporter protein (EGFP) and stably produced in Arabidopsis seedlings.…”

Section: Subcellular Localization Of the Atpra1 Proteins In Arabidopsismentioning

confidence: 99%

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ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

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Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the vacuolar soluble N-ethylmaleimide-sensitive factor attachment receptor protein VAMP2. However, little is known about PRA1 family members in plants. Sequence analysis revealed that higher plants, compared with animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis (Arabidopsis thaliana) PRA1 (AtPRA1) proteins were found to homodimerize and heterodimerize in a manner corresponding to their phylogenetic distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly coexpressed with Rab GTPases and genes encoding vesicle transport proteins, suggesting an involvement in the vesicle trafficking process similar to that of their animal counterparts. Correspondingly, AtPRA1 proteins were localized in the endoplasmic reticulum, Golgi apparatus, and endosomes/ prevacuolar compartments, hinting at a function in both secretory and endocytic intracellular trafficking pathways. Taken together, our data reveal a high functional diversity of AtPRA1 proteins, probably dealing with the various demands of the complex trafficking system.

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Section: Discussionmentioning

confidence: 87%

Section: Subcellular Localization Of the Atpra1 Proteins In Arabidopsismentioning

confidence: 99%

ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

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“…In addition to binding to Rabs, Pra1p binds to the SNARE Vamp2p (39). Although Pra1p localizes predominantly to Golgi membranes (41), it is also present at the presynaptic active zone where it is a component of the cytoskeletal matrix. There it interacts with Piccolo (42), a protein implicated in the regulation of Ca 2ϩ -mediated exocytosis (43).…”

Section: A Novel Role For the Yip1p Family In Membrane Fusion-mentioning

confidence: 99%

The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

Barrowman¹,

Wang²,

Zhang

et al. 2003

Journal of Biological Chemistry

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Here we report that Yip1p and Yif1p, two members of an integral membrane protein complex that bind to the Rab Ypt1p, are required for membrane fusion with the Golgi in vitro. To block fusion, anti-Yip1p or anti-Yif1p antibodies must be added before vesicles bud from the endoplasmic reticulum (ER). These antibodies do not block the packaging of Yip1p, Yif1p, or the soluble NSF attachment protein receptor (SNAREs) into vesicles. We propose that Yip1p and Yif1p perform a critical role in establishing the fusion competence of ER to Golgi vesicles at the time of budding. Consistent with this proposal, we observe that the Yip1p⅐Yif1p complex binds to the ER to Golgi SNAREs Bos1p and Sec22p, two components of the membrane fusion machinery.

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“…Additionally, PRA1 activates the dissociation of prenylated Rabs from the Rab/GDI complex, facilitating the association of prenylated Rabs with target membranes. This indicates that PRA1/Yip3 plays a role in targeting prenylated Rabs to their specific compartments by acting as a GDI displacement factor (Abdul-Ghani et al, 2001;Sivars et al, 2003;Seabra and Wasmeier, 2004). PRA1 also interacts with the SNARE protein VAMP2 and may play a role in regulating vesicle fusion to target membranes.…”

mentioning

confidence: 99%

“…PRA2 belongs to the Yip6 subfamily and localizes to the ER (Abdul-Ghani et al, 2001;Pfeffer and Aivazian, 2004). PRA2/PRA2F expression levels are elevated in various cancer cells, and the encoded proteins are enriched in synaptic vesicles in neuronal cells (Koomoa et al, 2008;Borsics et al, 2010).…”

mentioning

confidence: 99%

An Arabidopsis Prenylated Rab Acceptor 1 Isoform, AtPRA1.B6, Displays Differential Inhibitory Effects on Anterograde Trafficking of Proteins at the Endoplasmic Reticulum

et al. 2011

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Prenylated Rab acceptors (PRAs), members of the Ypt-interacting protein family of small membrane proteins, are thought to aid the targeting of prenylated Rabs to their respective endomembrane compartments. In plants, the Arabidopsis (Arabidopsis thaliana) PRA1 family contains 19 members that display varying degrees of sequence homology to animal PRA1 and localize to the endoplasmic reticulum (ER) and/or endosomes. However, the exact role of these proteins remains to be fully characterized. In this study, the effect of AtPRA1.B6, a member of the AtPRA1 family, on the anterograde trafficking of proteins targeted to various endomembrane compartments was investigated. High levels of AtPRA1.B6 resulted in differential inhibition of coat protein complex II vesicle-mediated anterograde trafficking. The trafficking of the vacuolar proteins sporamin:GFP (for green fluorescent protein) and AALP:GFP, the secretory protein invertase:GFP, and the plasma membrane proteins PMP:GFP and H + -ATPase:GFP was inhibited in a dose-dependent manner, while the trafficking of the Golgi-localized proteins ST:GFP and KAM1(DC):mRFP was not affected. Conversely, in RNA interference plants displaying lower levels of AtPRA1.B6 transcripts, the trafficking efficiency of sporamin:GFP and AALP:GFP to the vacuole was increased. Localization and N-glycan pattern analyses of cargo proteins revealed that AtPRA1.B6-mediated inhibition of anterograde trafficking occurs at the ER. In addition, AtPRA1.B6 levels were controlled by cellular processes, including 26S proteasome-mediated proteolysis. Based on these results, we propose that AtPRA1. B6 is a negative regulator of coat protein complex II vesicle-mediated anterograde trafficking for a subset of proteins at the ER.

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PRA Isoforms Are Targeted to Distinct Membrane Compartments

Cited by 74 publications

References 45 publications

ThePRA1Gene Family in Arabidopsis

ThePRA1Gene Family in Arabidopsis

The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

An Arabidopsis Prenylated Rab Acceptor 1 Isoform, AtPRA1.B6, Displays Differential Inhibitory Effects on Anterograde Trafficking of Proteins at the Endoplasmic Reticulum

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