<b>BIG2, A Guanine Nucleotide Exchange Factor for ADP-Ribosylation Factors: Its Localization to Recycling Endosomes and Implication in the Endosome Integrity</b>

Shin, Hye‐Won; Morinaga, Naoko; Noda, Masatoshi; Nakayama, Kazuhisa

doi:10.1091/mbc.e04-05-0388

Cited by 129 publications

(130 citation statements)

References 66 publications

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“…We found FIP3 interaction stimulates ASAP1 GAP activity against Arf1, but not against Arf6. In addition to its function at the Golgi apparatus, Arf1 is thought to have similar functions at other cellular locations such as TGN, endosome, and the plasma membrane (Shin et al, 2004;Pagano et al, 2004;D'Souza-Schorey and Chavrier, 2006;Cohen et al, 2007;Kumari and Mayor, 2008). A recent report has suggested a model in which Arf6 indirectly recruits activated Arf1 to the plasma membrane (Cohen et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…In control siRNA-transfected cells, we detected that a small amount of Arf1 and Arf6 on TfRpositive vesicles at perinuclear region, which becomes reduced upon the depletion of ASAP1. Because AP-1 and Arf guanine nucleotide exchange factor BIG2 act at the recycling endosome in addition to the TGN (Deneka et al, 2003;Shin et al, 2004), Arf1 as well as Arf6 may be involved in the function of the recycling endosome. In this context, ASAP1 may regulate Arf1 association to the recycling endosome and, as a consequence, the translocation of the endosomes from the pericentrosomal region to the cell periphery.…”

Section: Discussionmentioning

confidence: 99%

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Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Inoue

Prekeris

et al. 2008

MBoC

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ADP-ribosylation factors (Arfs) and Arf GTPase-activating proteins (GAPs) are key regulators of membrane trafficking and the actin cytoskeleton. The Arf GAP ASAP1 contains an N-terminal BAR domain, which can induce membrane tubulation. Here, we report that the BAR domain of ASAP1 can also function as a protein binding site. Two-hybrid screening identified FIP3, which is a putative Arf6-and Rab11-effector, as a candidate ASAP1 BAR domain-binding protein. Both coimmunoprecipitation and in vitro pulldown assays confirmed that ASAP1 directly binds to FIP3 through its BAR domain. ASAP1 formed a ternary complex with Rab11 through FIP3. FIP3 binding to the BAR domain stimulated ASAP1 GAP activity against Arf1, but not Arf6. ASAP1 colocalized with FIP3 in the pericentrosomal endocytic recycling compartment. Depletion of ASAP1 or FIP3 by small interfering RNA changed the localization of transferrin receptor, which is a marker of the recycling endosome, in HeLa cells. The depletion also altered the trafficking of endocytosed transferrin. These results support the conclusion that ASAP1, like FIP3, functions as a component of the endocytic recycling compartment. INTRODUCTIONArf family GTP-binding proteins and their GTPase-activating proteins (Arf GAPs) play crucial roles for membrane traffic and actin remodeling (D'Souza-Schorey and Chavrier, 2006;Gillingham and Munro, 2007). Arf GAPs share the same catalytic domain, the Arf GAP domain, which is responsible for GTP hydrolysis. In humans, 31 genes encoding proteins with Arf GAP domains have been found. They are classified into several subfamilies based on their domain structures Inoue and Randazzo, 2007). Three subfamilies, ArfGAPs, SMAPs, and GITs, have an Arf GAP domain at the N-terminus of the molecules. In contrast, the others, which are called AZAP-family Arf GAPs, contain an Arf GAP domain following a pleckstrin homology (PH) domain in the middle of the protein. They are subdivided into four subfamilies, ASAPs, ACAPs, ARAPs, and AGAPs.ASAP1 is one of the best-characterized Arf GAPs. In addition to PH and Arf GAP domains, ASAP1 contains an N-terminal Bin, Amphiphysin, and Rvs167/Rvs161 (BAR) domain and, in the C-terminal half of the protein, a proline (Pro)-rich domain and Src homology 3 (SH3) domain. Other ASAP isoforms, ASAP2 and ASAP3, have similar domain structures and high homology, especially in the Arf GAP domains, although ASAP3 lacks C-terminal SH3 domain (Ha et al., 2008). Through its Pro-rich and SH3 domains, ASAP1 interacts with a number of proteins, which are mainly adhesion-and actin cytoskeleton-related proteins including Src, focal adhesion kinase (FAK), Crk/CrkL, and cortactin (Brown et al., 1998;Liu et al., 2002;Oda et al., 2003;Onodera et al., 2005;Bharti et al., 2007). ASAP1 is a component of three integrated membrane/actin cytoskeleton structures: focal adhesions, circular dorsal ruffles (CDRs) and invadopodia/podosomes. ASAP1 associates with focal adhesions in fibroblasts . The focal adhesion localization depends on the interaction of ASAP1 with FA...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Inoue

Prekeris

et al. 2008

MBoC

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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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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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“…1d). To discriminate whether hRAB37 was involved in secretion or endocytic recycling, we also performed quantitative analyses for the recycling of endocytosed transferrin receptor (TfnR) 24,25 (Fig. 1e).…”

Section: Hrab37 Is Involved In Transportation Of Exocytotic Vesiclesmentioning

confidence: 99%

Small GTPase Rab37 targets tissue inhibitor of metalloproteinase 1 for exocytosis and thus suppresses tumour metastasis

et al. 2014

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Rab small GTPases are master regulators of membrane trafficking and guide vesicle targeting. Recent publications show that Rab-controlled trafficking pathways are altered during tumorigenesis. However, whether any of the Rabs plays a metastasis suppressor role is least explored. Here we address the metastasis suppressive function of human Rab37 (hRAB37) using secretomics, cell, animal and clinical analyses. We show that tissue inhibitor of metalloproteinase 1 (TIMP1), a secreted glycoprotein that inhibits extracellular matrix turnover, is a novel cargo of hRAB37. hRAB37 regulates the exocytosis of TIMP1 in a nucleotide-dependent manner to inactivate matrix metalloproteinase 9 (MMP9) migration axis in vitro and in vivo. Dysfunction of hRAB37 or TIMP1 abrogates metastasis suppression. Lung cancer patients with metastasis and poor survival show low hRAB37 protein expression coinciding with low TIMP1 in tumours. Our findings identify hRAB37 as a novel metastasis suppressor Rab that functions through the TIMP1-MMP9 pathway and has significant prognostic power.

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BIG2, A Guanine Nucleotide Exchange Factor for ADP-Ribosylation Factors: Its Localization to Recycling Endosomes and Implication in the Endosome Integrity

Cited by 129 publications

References 66 publications

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

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

Small GTPase Rab37 targets tissue inhibitor of metalloproteinase 1 for exocytosis and thus suppresses tumour metastasis

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