Regulators and effectors of the ARF GTPases

Current Opinion in Cell Biology

Volumn 12, Issue 4, 2000, Pages 475-482

  Donaldson, Julie G ^a   Jackson, Catherine L ^b  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^b CEA SACLAY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; COAT PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE KINASE;

CELL MEMBRANE; ENZYME REGULATION; PRIORITY JOURNAL; REVIEW;

EID: 0033937941     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00119-8     Document Type: Review

References (70)

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16. Claude A., Zhao B.P., Kuziemsky C.E., Dahan S., Berger S.J., Yan J.P., Armold A.D., Sullivan E.M., Melanon P. GBF1. A novel golgi-associated bfa-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J Cell Biol. 146:1999;71-84. This paper reports the identification of GBF1, a novel 206 kDa ARF GEF that colocalizes with β-COP at the Golgi apparatus. Overexpression of GBF1 in mammalian cells confers resistance to the growth inhibition and Golgi disassembly caused by treatment with BFA. Surprisingly, partially purified GBF1 does not have in vitro exchange activity on Class I ARFs but acts as a GEF on the Class II member ARF5. This activity is BFA-resistant.
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23. Geiger C., Nagel W., Boehm T., van Kooyk Y., Figdor C.G., Kremmer E., Hogg N., Zeitlmann L., Dierks H., Weber K.S.C., Kolanus W. Cytohesin-1 regulates beta-2 integrin mediated cell adhesion through both ARF-GEF function and direct interaction with LFA-1. EMBO J. 2000;. in press. The ARF GEF cytohesin-1 regulates inside-out signalling through its interaction with the β-2 integrin LFA-1. Overexpression of cytohesin-1 in Jurkat cells induces cell adhesion and cell spreading, and the authors show here that this effect is abrogated when the inactivating E157K mutation is introduced into the cytohesin-1 Sec7 ARF GEF domain.
24. Santy L.C., Frank S.R., Hatfield J.C., Casanova J.E. Regulation of ARNO nucleotide exchange by a PH domain electrostatic switch. Curr Biol. 9:1999;1173-1176. The ARF GEF ARNO is recruited to membranes through its PH domain and an adjacent polybasic domain. Here, these authors show that phosphorylation of a serine residue within the polybasic region by PKC negatively regulates ARNO activity by inhibiting its membrane binding both in vitro and in vivo.
25. 32P-orthophosphate labelling of cells and immunoprecipitation that overexpression of the ARF GEFs GRP1 and cytohesin-1 leads to a greater increase in the amount of ARF6-GTP in cells than of ARF1-GTP. These results support the conclusion that GRP1 and cytohesin-1 can act as exchange factors for ARF6 in vivo.
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30. Randazzo P.A., Andrade J., Miura K., Brown M.T., Long Y.Q., Stauffer S., Roller P., Cooper J.A. The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton. Proc Natl Acad Sci USA. 97:2000;4011-4016. Endogenous ASAP1 localizes to focal adhesions and move into membrane ruffles in cells treated with PDGF. Overexpression of wild-type ASAP1, but not a mutated catalytically inactive GAP, inhibits PDGF ruffling and cell spreading. As ASAP1 binds to, and is phosphorylated by, src, it might couple signal transduction events with coordination of membrane traffic and actin dynamics.
31. Mandiyan V., Andreev J., Schlessinger J., Hubbard S.R. Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta. EMBO J. 18:1999;6890-6898. The crystal structure of the PAPβ ARF GAP domain and ankyrin repeats was determined at 2.1Å. An invariant arginine and adjacent hydrophobic residues were found to be solvent exposed and the authors predict this to be the ARF-interaction site. Mutation of these residues results in a loss of GAP activity. This proposed mechanism, which invokes an arginine finger in catalysis, contrasts with that proposed by J Goldberg for ARF GAP1 [32].
32. Goldberg J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell. 96:1999;893-902.
33. Springer S., Spang A., Schekman R. A primer on vesicle budding. Cell. 97:1999;145-148.
34. Goldberg J. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Cell. 100:2000;671-679. In a previous study [32], Goldberg showed that coatomer stimulates ARF GAP1-mediated GTP hydrolysis on ARF1. Here he shows that a synthetic peptide corresponding to the carboxy-terminal region of a transmembrane COPI vesicle cargo protein (a member of the p24 family), inhibits coatomer stimulation of ARF GAP1 activity. Goldberg proposes a model in which cargo sorting by COPI is accomplished by kinetic control of the GTPase reaction.
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43. 3.
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48. Blader I.J., Cope M.J., Jackson T.R., Profit A.A., Greenwood A.F., Drubin D.G., Prestwich G.D., Theibert A.B. GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Mol Biol Cell. 10:1999;581-596. This study supports a role for ARF GAPs in actin organization in yeast. Deletion of Gcs1, an ARF GAP implicated in ER-Golgi trafficking in yeast (see [38]), results in altered actin structures, increased sensitivity to latrunculin B, and synthetic lethality with deletion of SLA2, a gene implicated in actin stabilization. In addition to a GAP domain, Gcs1 has PH and ERM (ezrin-radixin-moesin) domains. Gcs1 is also shown to bind to actin filaments and to stimulate actin polymerization in vitro.
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57. •].
58. •] also showed that the GGAs are not components of AP1-clathrin-coated vesicles and that in yeast the loss of the two GGAs causes aberrant vacuolar morphology. Both groups showed missorting of the vacuolar hydrolase CPY in gga1Δ gga2Δ double mutants.
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62. •].
63. •]. These studies provide more evidence of ARF acting on other targets in addition to coat proteins.
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