Structural Basis for Arl1-Dependent Targeting of Homodimeric GRIP Domains to the Golgi Apparatus

Panić, B.; Perišić, Olga; Veprintsev, Dmitry B.; Williams, Roger L.; Munro, Sean

doi:10.1016/s1097-2765(03)00356-3

Cited by 132 publications

(177 citation statements)

References 60 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%

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%

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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“…As predicted from sequence signatures, 22 structural studies of Arf-like and Arf-related GTPases, including Golgi Arl1, 74,75 cilium Arl3 76,77,78 and Arl6 79 and endoplasmic reticulum Sar1 80,81 have now shown that autoinhibition by the N-terminal extension and the interswitch takes place in these GTPases and is released by the displacement of the N-terminus and the toggle of the interswitch. Thus, the allosteric mechanism that uses the displacement of the N-terminal extension as a priming event to autoinhibition release and the remodeling of the interswitch as the means whereby information is propagated to the nucleotide-binding site is probably general to the entire Arf-like family.…”

Section: Regulation Of Bacterial Arfgefs By Membranesmentioning

confidence: 80%

Allosteric regulation of Arf GTPases and their GEFs at the membrane interface

2016

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Arf GTPases assemble protein complexes on membranes to carry out major functions in cellular traffic. An essential step is their activation by guanine nucleotide exchange factors (GEFs), whose Sec7 domain stimulates GDP/GTP exchange. ArfGEFs form 2 major families: ArfGEFs with DCB, HUS and HDS domains (GBF1 and BIG1/BIG2 in humans), which act at the Golgi; and ArfGEFs with a Cterminal PH domain (cytohesin, EFA6 and BRAG), which function at the plasma membrane and endosomes. In addition, pathogenic bacteria encode an ArfGEF with a unique membrane-binding domain. Here we review the allosteric regulation of Arf GTPases and their GEFs at the membrane interface. Membranes contribute several regulatory layers: at the GTPase level, where activation by GTP is coupled to membrane recruitment by a built-in structural device; at the Sec7 domain, which manipulates this device to ensure that Arf-GTP is attached to membranes; and at the level of noncatalytic ArfGEF domains, which form direct or GTPase-mediated interactions with membranes that enable a spectacular diversity of regulatory regimes. Notably, we show here that membranes increase the efficiency of a large ArfGEF (human BIG1) by 32-fold by interacting directly with its Nterminal DCB and HUS domains. The diversity of allosteric regulatory regimes suggests that ArfGEFs can function in cascades and circuits to modulate the shape, amplitude and duration of Arf signals in cells. Because Arf-like GTPases feature autoinhibitory elements similar to those of Arf GTPases, we propose that their activation also requires allosteric interactions of these elements with membranes or other proteins.

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“…We and others recently demonstrated that GRIP Golgins form homodimers through both their GRIP and coiled-coil regions (Panic et al, 2003a;Wu et al, 2004). Similar to p115, GM130 and Giantin, the homodimer of Golgin-97 probably adopt a long rod structure, with its C-terminal GRIP domain anchoring to the TGN membrane through interaction with two Arl1-GTP, whereas its N-terminal globular regions extend into the cytosol to mediate the tethering of retrograde transport vesicles derived from endosomes.…”

Section: Discussionmentioning

confidence: 94%

Autoantigen Golgin-97, an Effector of Arl1 GTPase, Participates in Traffic from the Endosome to theTrans-Golgi Network

Lü

Tai

Hong

2004

MBoC

162

147

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The precise cellular function of Arl1 and its effectors, the GRIP domain Golgins, is not resolved, despite our recent understanding that Arl1 regulates the membrane recruitment of these Golgins. In this report, we describe our functional study of Golgin-97. Using a Shiga toxin B fragment (STxB)-based in vitro transport assay, we demonstrated that Golgin-97 plays a role in transport from the endosome to the trans-Golgi network (TGN). The recombinant GRIP domain of Golgin-97 as well as antibodies against Golgin-97 inhibited the transport of STxB in vitro. Membrane-associated Golgin-97, but not its cytosolic pool, was required in the in vitro transport assay. The kinetic characterization of inhibition by anti-Golgin-97 antibody in comparison with anti-Syntaxin 16 antibody established that Golgin-97 acts before Syntaxin 16 in endosome-to-TGN transport. Knock down of Golgin-97 or Arl1 by their respective small interference RNAs (siRNAs) also significantly inhibited the transport of STxB to the Golgi in vivo. In siRNA-treated cells with reduced levels of Arl1, internalized STxB was instead distributed peripherally. Microinjection of Golgin-97 antibody led to the fragmentation of Golgi apparatus and the arrested transport to the Golgi of internalized Cholera toxin B fragment. We suggest that Golgin-97 may function as a tethering molecule in endosome-to-TGN retrograde traffic. INTRODUCTIONIn eukaryotic cells, different types of cargo (solutes, lipids, and membrane proteins, including receptors and their ligands) internalized from the plasma membrane follow several routes upon reaching the early/sorting endosome. They could recycle back to the plasma membrane directly via early/sorting endosome or indirectly via the recycling endosome, or travel further to the lysosome via the late endosome. Recently, there was evidence suggesting the existence of two retrograde transport pathways from endosomes to the trans-Golgi network (TGN) (Ghosh et al., 1998;Mallard et al., 1998;Mallet and Maxfield, 1999). One pathway, used by furin (Mallet and Maxfield, 1999) and mannose-6-phosphate receptor (M6PR) (Diaz and Pfeffer, 1998;Sincock et al., 2003), is from the late endosome to the TGN. The other one, used by TGN38 (Ghosh et al., 1998), Shiga Toxin B fragment (STxB) (Mallard et al., 1998) and likely GLUT4 (Shewan et al., 2003), proceeds via the early endosome (EE) and/or the recycling endosome (RE), without passing through late endosomes. In addition, the large cation-independent M6PR and the small cation-dependent MPR46 are recently shown to also use this EE/RE-TGN pathway, in addition to its well characterized late endosome-TGN route (Medigeshi and Schu, 2003;Lin et al., 2004). These endosome-TGN pathways could be used by other proteins such as P-selectin (Straley and Green, 2000), membrane-type matrix metalloproteinases (Kang et al., 2002;Zucker et al., 2002;Remacle et al., 2003; Wang et al., 2004a,b), copper transporters (Petris and Mercer, 1999;Petris et al., 2002), and VAMP4, a TGN SNARE (unpublished observations). In addition, ...

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Structural Basis for Arl1-Dependent Targeting of Homodimeric GRIP Domains to the Golgi Apparatus

Cited by 132 publications

References 60 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

Allosteric regulation of Arf GTPases and their GEFs at the membrane interface

Autoantigen Golgin-97, an Effector of Arl1 GTPase, Participates in Traffic from the Endosome to theTrans-Golgi Network

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