Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking

Shin, Hye‐Won; Kobayashi, Hiromi; Kitamura, Masashi; Waguri, Satoshi; Suganuma, Tatsuo; Uchiyama, Yasuo; Nakayama, Kazuhisa

doi:10.1242/jcs.02524

Cited by 79 publications

(79 citation statements)

References 57 publications

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“…Based on data in vitro data from cultured cells transfected with ARFRP1 constructs, we and others have previously suggested that the GTPase is required for targeting of ARL1 and of its effector Golgin-245 to the trans-Golgi network (7)(8)(9)(10)43). The present data provide solid proof for this conclusion in showing that ARL1 dissociated from Golgi membranes to the cytosol in an in vivo knockdown of Arfrp1 (Arfrp1 vilϪ/Ϫ epithelial cells, Fig.…”

Section: Discussionsupporting

confidence: 82%

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ADP-ribosylation Factor-like GTPase ARFRP1 Is Required for Trans-Golgi to Plasma Membrane Trafficking of E-cadherin

Zahn

Jaschke

Weiske

et al. 2008

Journal of Biological Chemistry

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ADP-ribosylation factor-related protein 1 (ARFRP1) plays a specific role in Golgi function controlling recruitment of GRIP domain proteins and ARL1 to the trans-Golgi. Deletion of the mouse Arfrp1 gene causes embryonic lethality during early gastrulation, because epiblast cells detach from the ectodermal cell layer and do not differentiate to mesodermal tissue. Here we show that in Arfrp1 ؊/؊ embryos E-cadherin is mistargeted to intracellular compartments, whereas in control embryos it is present at the cell surface of trophectodermal and ectodermal cells. In enterocytes of intestine-specific Arfrp1 null mutants (Arfrp1), E-cadherin is associated with intracellular membranes, partially colocalizing with the cis-Golgi marker GM130 or with punctae close to the cell surface. In contrast, in control enterocytes E-cadherin is exclusively located in the lateral membranes. In addition, ARL1 is dislocated from Golgi membranes to the cytosol of Arfrp1 vil؊/؊ enterocytes. Depletion of endogenous ARFRP1 by RNA interference leads to a dislocation of E-cadherin from the cell surface in HeLa cells and to a reduced cell aggregation in Ltk ؊ Ecad cells. ARFRP1 was coimmunoprecipitated in a complex with E-cadherin, ␣-catenin, ␤-catenin, ␥-catenin, and p120 ctn from lysates of MadinDarby canine kidney cells stably expressing myc-ARFRP1. These data indicate that knock-out of Arfrp1 disrupts the trafficking of E-cadherin through the Golgi and suggest an essential role of the GTPase in trans-Golgi network function.

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Section: Discussionsupporting

confidence: 82%

“…We and others have recently shown that ARFRP1 as well as its yeast ortholog Arl3p specifically control targeting of ARL1 and its effector Golgin-245 to the trans-Golgi (7)(8)(9)(10). GTPbound ARFRP1 (ARFRP1-Q79L mutant) was associated with Golgi membranes and colocalized with ARL1.…”

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confidence: 99%

ADP-ribosylation Factor-like GTPase ARFRP1 Is Required for Trans-Golgi to Plasma Membrane Trafficking of E-cadherin

Zahn

Jaschke

Weiske

et al. 2008

Journal of Biological Chemistry

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“…Cell Culture, siRNA-mediated Knockdown, and Immunofluorescence Analysis-Culture of HeLa cells and transfection of expression plasmids were performed as described previously (29,30). RPE1 cells were grown in a 1:1 mixture of Dulbecco's modified Eagle's medium and Ham's F-12 medium supplemented with 10% heat-inactivated fetal calf serum, 2 mM L-glutamine, 100 units/ml penicillin, and 100 g/ml streptomycin.…”

Section: Methodsmentioning

confidence: 99%

ATP9B, a P4-ATPase (a Putative Aminophospholipid Translocase), Localizes to the trans-Golgi Network in a CDC50 Protein-independent Manner

Takatsu

Baba

Shima

et al. 2011

Journal of Biological Chemistry

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118

135

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Type IV P-type ATPases (P4-ATPases) are putative phospholipid flippases that translocate phospholipids from the exoplasmic (lumenal) to the cytoplasmic leaflet of lipid bilayers and are believed to function in complex with CDC50 proteins. In Saccharomyces cerevisiae, five P4-ATPases are localized to specific cellular compartments and are required for vesicle-mediated protein transport from these compartments, suggesting a role for phospholipid translocation in vesicular transport. The human genome encodes 14 P4-ATPases and three CDC50 proteins. However, the subcellular localization of human P4-ATPases and their interactions with CDC50 proteins are poorly understood. Here, we show that class 5 (ATP10A, ATP10B, and ATP10D) and class 6 (ATP11A, ATP11B, and ATP11C) P4-ATPases require CDC50 proteins, primarily CDC50A, for their exit from the endoplasmic reticulum (ER) and final subcellular localization. In contrast, class 2 P4-ATPases (ATP9A and ATP9B) are able to exit the ER in the absence of exogenous CDC50 expression: ATP9B, but not ATP11B, was able to exit the ER despite depletion of CDC50 proteins by RNAi. Although ATP9A and ATP9B show a high overall sequence similarity, ATP9A localizes to endosomes and the trans-Golgi network (TGN), whereas ATP9B localizes exclusively to the TGN. A chimeric ATP9 protein in which the N-terminal cytoplasmic region of ATP9A was replaced with the corresponding region of ATP9B was localized exclusively to the Golgi. These results indicate that ATP9B is able to exit the ER and localize to the TGN independently of CDC50 proteins and that this protein contains a Golgi localization signal in its N-terminal cytoplasmic region.In eukaryotic cells, the lipid bilayer of the plasma membrane as well as membranes of secretory and endocytic compartments exhibits asymmetric lipid distributions; aminophospholipids, phosphatidylserine (PS), 3 and phosphatidylethanolamine are concentrated in the cytoplasmic leaflet (1, 2). For example, in resting human red blood cells, PS and phosphatidylethanolamine are restricted primarily to the inner leaflet of the plasma membrane, whereas phosphatidylcholine and sphingomyelin are exposed on the cell surface (3, 4). Regulated exposure of PS in the outer leaflet occurs in many biological processes, such as apoptotic cell death, platelet coagulation reactions, and the fusion of muscle (4 -7); similarly, phosphatidylethanolamine is exposed on the surface of the cleavage furrow during cytokinesis (8). In addition, phospholipid asymmetry of the bile canalicular membrane is critical to membrane integrity and normal bile secretion by hepatocytes (9); loss of phospholipid asymmetry due to mutations in the human FIC1/ATP8B1 (a member of the P4-ATPase family) gene causes a liver disease, progressive familial intrahepatic cholestasis (10).P4-ATPases are a subfamily of P-type ATPases and have been implicated in flipping aminophospholipids from the exoplasmic (lumenal) leaflet to the cytoplasmic leaflet (11-15). The yeast P4-ATPases (Drs2p, Neo1p, Dnf1p, Dnf2p, and Dnf3p) a...

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“…Culture of HeLa cells and transfection of expression plasmids were performed as described previously (Shin et al, 2005. HeLa cell lines stably expressing TfnR-EGFP were established as described previously .…”

Section: Antibodies and Reagentsmentioning

confidence: 99%

ARF1 and ARF3 Are Required for the Integrity of Recycling Endosomes and the Recycling Pathway

Kondo

Hanai

Nakai

et al. 2012

Cell Struct. Funct.

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ABSTRACT. Small GTPases ARF1 and ARF3 localize mainly to the Golgi apparatus, where they trigger formation of coated carrier vesicles. We previously showed that BIG2, a guanine nucleotide exchange factor specific for ARF1 and ARF3, localizes not only to the trans-Golgi network (TGN) but also to recycling endosomes, where it is involved in regulating the integrity of recycling endosomes. However, it is not yet clear whether ARF1 and ARF3 act downstream of BIG2 to ensure endosome integrity. In this study, we show that EGFP-tagged ARF1 and ARF3 localize to endosomal compartments containing endocytosed transferrin. We further demonstrate that simultaneous depletion of ARF1 and ARF3 induces tubulation of recycling endosomal compartments positive for transferrin receptor, Rab4, and Rab11, but does not significantly affect the integrity of the Golgi apparatus or early or late endosomes. Moreover, the simultaneous depletion of ARF1 and ARF3 suppresses recycling of transferrin but does not affect either its endocytosis or the retrograde transport of TGN38 from early/recycling endosomes to the TGN. In addition, depletion of ARF1 and ARF3 does not affect retrograde transport of CD4-furin from late endosomes to the TGN, or of endocytosed EGF from late endosomes to lysosomes. These results indicate that ARF1 and ARF3 are redundantly required for the integrity of recycling endosomes, and that they regulate transferrin recycling from endosomes to the plasma membrane, but not retrograde transport from endosomal compartments to the TGN.

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Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking

Cited by 79 publications

References 57 publications

ADP-ribosylation Factor-like GTPase ARFRP1 Is Required for Trans-Golgi to Plasma Membrane Trafficking of E-cadherin

ADP-ribosylation Factor-like GTPase ARFRP1 Is Required for Trans-Golgi to Plasma Membrane Trafficking of E-cadherin

ATP9B, a P4-ATPase (a Putative Aminophospholipid Translocase), Localizes to the trans-Golgi Network in a CDC50 Protein-independent Manner

ARF1 and ARF3 Are Required for the Integrity of Recycling Endosomes and the Recycling Pathway

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