Arf3 Is Activated Uniquely at the<i>trans</i>-Golgi Network by Brefeldin A-inhibited Guanine Nucleotide Exchange Factors

Manolea, Florin; Chun, Justin; Chen, David W.; Clarke, Ian E.; Summerfeldt, Nathan; Dacks, Joel B.; Melançon, Paul

doi:10.1091/mbc.e10-01-0016

Cited by 53 publications

(80 citation statements)

References 72 publications

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“…5A) (Cavenagh et al, 1996;Kawamoto et al, 2002;Manolea et al, 2010), here we have used time-lapse imaging to demonstrate the endosomal localization of ARF1-EGFP and ARF3-EGFP exogenously expressed in cells depleted of endogenous ARF1 and/or ARF3. We believe that some populations of ARF1 and ARF3 localize to TfnRpositive endosomes as well as to the Golgi; that their membrane association is saturable; and that membrane association of ARF1 is more stable than that of ARF3, on the basis of the following observations: (i) Endosomal localization of ARF1-EGFP is detectable in ARF1-depleted cells; (ii) endosomal localization of ARF3-EGFP is observed in cells depleted of both ARF1 and ARF3, but not in cells depleted of ARF3 alone; and (iii) endosomal localization of the ARF3(FF)-EGFP mutant, which has a larger hydrophobic surface and is less temperature-sensitive than ARF3-WT (Manolea et al, 2010), is detectable in ARF3-depleted cells.…”

Section: Discussionmentioning

confidence: 99%

“…5B, bottom panels, and supplemental Video S7). In light of a recent report showing that ARF3(FF)-EGFP is recruited onto membranes more efficiently than ARF3-EGFP (Manolea et al, 2010), it is likely that ARF1 binds more effectively than ARF3 to endosomal membranes, due to the bulky aromatic amino acids in the N-terminal amphipathic helix; however, the precise molecular details remain unknown. Overall, these observations indicate that some populations of ARF1 and ARF3 are associated with membranes of Tfn-positive endosomes as well as with Golgi membranes (see Discussion).…”

Section: Arf1 and Arf3 Localize To Tfn-positive Endosomes As Well As mentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Arf1 and Arf3 Localize To Tfn-positive Endosomes As Well As mentioning

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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“…There are three classes of Arf proteins in mammals, based largely on sequence homology -Class I (Arfs1-3), Class II (Arfs 4-5) and Class III (Arf6). Class I Arfs are highly conserved and are present in all eukaryotes, whereas the Class II Arfs arose during animal cell evolution, diverging from the Class I Arfs in the animal lineage after fungi separated, but before multicellular organisms arose (Manolea et al, 2010;Schlacht et al, 2013). Class III Arfs are ancient but, unlike Class I Arfs, are more divergent, especially in plants (Gebbie et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Arfs at a Glance

Jackson

Bouvet

2014

Journal of Cell Science

119

117

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The Arf small G proteins regulate protein and lipid trafficking in eukaryotic cells through a regulated cycle of GTP binding and hydrolysis. In their GTP-bound form, Arf proteins recruit a specific set of protein effectors to the membrane surface. These effectors function in vesicle formation and tethering, non-vesicular lipid transport and cytoskeletal regulation. Beyond fundamental membrane trafficking roles, Arf proteins also regulate mitosis, plasma membrane signaling, cilary trafficking and lipid droplet function. Tight spatial and temporal regulation of the relatively small number of Arf proteins is achieved by their guanine nucleotideexchange factors (GEFs) and GTPase-activating proteins (GAPs), which catalyze GTP binding and hydrolysis, respectively. A unifying function of Arf proteins, performed in conjunction with their regulators and effectors, is sensing, modulating and transporting the lipids that make up cellular membranes. In this Cell Science at a Glance article and the accompanying poster, we discuss the unique features of Arf small G proteins, their functions in vesicular and lipid trafficking in cells, and how these functions are modulated by their regulators, the GEFs and GAPs. We also discuss how these Arf functions are subverted by human pathogens and disease states.

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“…One key group of small GTPases involved in membrane trafficking is the Arfs, consisting in humans of class I (Arf1 and Arf3), class II (Arf4 and Arf5) and class III (Arf6), with class I and II Arfs functioning in COPI-mediated membrane trafficking (D'Souza-Schorey and Chavrier, 2006). Arfs are recruited to the membranes of the Golgi and the ERGIC in a GDP-bound form (Gommel et al, 2001;Honda et al, 2005;Manolea et al, 2010), and they are subsequently activated (entering a GTP-bound form) through the actions of guanine-nucleotide-exchange factors (GEFs). Activated Arfs bind to COPI proteins, recruiting COPI coats to the membrane (Donaldson et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Scyl1 scaffolds class II Arfs to selective subcomplexes of coatomer via the γ-COP appendage domain

Hamlin

Schroeder

Fotouhi

et al. 2014

Journal of Cell Science

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Coatomer (COPI)-coated vesicles mediate membrane trafficking in the early secretory pathway. There are at least three subclasses of COPI coats and two classes of Arf GTPases that couple COPI coat proteins to membranes. Whether mechanisms exist to link specific Arfs to specific COPI subcomplexes is unknown. We now demonstrate that Scy1-like protein 1 (Scyl1), a member of the Scy1-like family of catalytically inactive protein kinases, oligomerizes through centrally located HEAT repeats and uses a C-terminal RKXX-COO 2 motif to interact directly with the appendage domain of coatomer subunit c-2 (also known as COPG2 or c2-COP). Through a distinct site, Scyl1 interacts selectively with class II Arfs, notably Arf4, thus linking class II Arfs to c2-bearing COPI subcomplexes. Therefore, Scyl1 functions as a scaffold for key components of COPI coats, and disruption of the scaffolding function of Scyl1 causes tubulation of the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) and the cisGolgi, similar to that observed following the loss of Arf and Arf-guaninenucleotide-exchange factor (GEF) function. Our data reveal that Scyl1 is a key organizer of a subset of the COPI machinery.

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Arf3 Is Activated Uniquely at thetrans-Golgi Network by Brefeldin A-inhibited Guanine Nucleotide Exchange Factors

Cited by 53 publications

References 72 publications

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

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

Arfs at a Glance

Scyl1 scaffolds class II Arfs to selective subcomplexes of coatomer via the γ-COP appendage domain

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