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ARF family

T H E J O U R N A L O F C E L L B I O L O G Y

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The Journal of Cell Biology, Vol. 172, No. 5, February 27, 2006 645–650https://www.wendangku.net/doc/584043556.html,/cgi/doi/10.1083/jcb.200512057

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Arf family history: Arfs, Arls, SARs, and other members

Arfs. Arf was fi rst discovered, purifi ed, and functionally de-

fi ned as the protein cofactor required for cholera toxin–catalyzed ADP ribosylation of the stimulatory regulatory subunit (Gs) of adenylyl cyclase (Enomoto and Gill, 1980; Kahn and Gilman, 1984) and, shortly thereafter, was shown to be a GTP-binding protein (K ahn and Gilman, 1986). Use of the acronym Arf is currently preferred to ADP ribosylation factor, as only Arf1–6 shares the cofactor activity for cholera toxin and because ADP ribosylation does not appear to be involved in any aspect of the normal cellular actions of any member of the family. The use of all capital letters (e.g., ARF1) refers specifi cally to the human gene or protein, whereas when only the fi rst letter is capitalized (e.g., Arf1), it may refer to the protein from more than one spe-cies, an activity, or a group of proteins. Since their discovery,

they have been found to be ubiquitous regulators of membrane traffi c and phospholipid metabolism in eukaryotic cells (for re-views and discussion of Arf actions see Nie et al., 2003; Burd et al., 2004; Kahn, 2004). Arfs are soluble proteins that translocate onto membranes in concert with their activation, or GTP bind-ing. The biological actions of Arfs are thought to occur on mem-branes and to result from their specifi c interactions with a large number of effectors that include coat complexes (COPI, AP-1, and AP-3), adaptor proteins (GGA1-3 and MINT1-3/X11α-γ/APBA1-3), lipid-modifying enzymes (PLD1, phosphatidylino-sitol (4,5)-kinase, and phosphatidylinositol (4)-kinase), and oth-ers. Arf proteins are activated by guanosine diphosphate (GDP) to GTP exchange, which is stimulated by the Sec7 domain of Arf guanine nucleotide exchange factors, and their activity is termi-nated upon the hydrolysis of GTP, which is stimulated by inter-action with an Arf GTPase-activating protein.

Cloning and sequencing of the fi rst Arf family member (Sewell and K ahn, 1988) led directly to the realization that Arfs are closely related to both the Ras and heterotrimeric G protein α subunit families of GTPases, and all are thought to have arisen from a common ancestor. The very high degree of conservation of Arf sequences in eukaryotes (74% between human and yeast) was also noted early on and has allowed the ready identifi cation of orthologues in every examined eukary-ote, including Giardia lamblia , which lack Ras and G protein α subunits (Murtagh et al., 1992).

Cloning by low stringency hybridization and chance led to the identifi cation of additional members of the Arf family in a wide array of eukaryotic species. The number of mammalian Arfs grew to six by 1992 (Tsuchiya et al., 1991) and were named in their order of discovery (Price et al., 1988; Bobak et al., 1989; Kahn et al., 1991; Lee et al., 1992). The fi rst confusion in the nomenclature was that the current human ARF4 was originally published with the name ARF2 (Kahn, et al., 1991). In fact, hu-mans appear to have lost the ARF2 orthologue, which is present in other mammals (including rats, mice, and cows). The combi-nation of protein sequence comparisons and intron/exon bound-aries of Arf genes led to further classifi cation of the six mammalian Arfs into classes: class I (ARF1–3 are >96% iden-tical), class II (ARF4 and ARF5 are 90% identical to each other

N omenclature for the human Arf family

of GTP-binding proteins: ARF , ARL, and SAR proteins

Richard A. Kahn,1 Jacqueline Cher? ls,2 Marek Elias,3 Ruth C. Lovering,4 Sean Munro,5 and Annette Schurmann 6

1Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322

2

Laboratoire d’Enzymologie et Biochimie Structurales, Centre National de la Recherche Scienti? que, 91198 Gif-sur-Yvette, France 3

Department of Plant Physiology, Faculty of Science, Charles University, 128 44 Prague 2, Czech Republic 4

Human Genome Organisation Gene Nomenclature Committee, Galton Laboratory, Department of Biology, University College London, London NW1 2HE, United Kingdom 5

Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom 6

Department of Pharmacology, German Institute of Human Nutrition Potsdam-Rehbrücke, D-14558 Nuthetal, Germany

The Ras supe rfamily is comprise d of at le ast four large familie s of re gulatory guanosine triphosphate –binding proteins, including the Arfs. The Arf family includes three different groups of proteins: the Arfs, Arf-like (Arls), and SARs. Several Arf family members have been very highly conse rve d throughout e ukaryotic e volution and have orthologues in evolutionally diverse species. The different means by which Arf family members have been identi? ed have re sulte d in an inconsiste nt and confusing array of name s. This confusion is furthe r compounde d by diffe r-e nce s in nome nclature be twe e n diffe re nt spe cie s. We propose a more consiste nt nome nclature for the human mem

b ers of the Arf family that may also serve as a guide for nomenclature in other species.

Correspondence to Richard A. Kahn: rkahn@https://www.wendangku.net/doc/584043556.html,

Abbreviations used in this paper: GDP , guanosine diphosphate; TRIM, tripartite motif.

The online version of this article contains supplemental material.

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Supplemental Material can be found at:

and 80% identical to the other Arfs), and class III (ARF6 is 64–69% identical to the other Arfs). Phylogenetic analyses support the conclusion that the three classes of Arf diverged early, as fl ies and worms have single representatives of each of the three classes, and the number of genes/proteins in class I and II were later expanded in vertebrates.

Arls. The initial criteria for naming new Arfs were func-tional, and only those proteins that could (1) serve as cofactors for cholera toxin, (2) rescue the lethal arf1?arf2? deletion in Saccharomyces cerevisiae, and (3) directly activate PLD were given the name Arf. Thus, with the chance cloning of an essential gene in Drosophila melanogaster that encoded a protein closely related to the Arfs (50–60% identity) but lacking in these activ-ities, it was named arfl ike (Tamkun et al., 1991). When ortho-logues were found in several other species, the name was changed to Arf-like 1 (ARL1) in those species (Kahn et al., 1992; Breiner et al., 1996; Lowe et al., 1996). Note that although the name Arf still denotes a protein with one or more specifi c functions or ac-tivities, the term Arl does not. The term Arl indicates only that the protein is structurally related to Arfs. Thus, the Arls are not a coherent group either functionally or phylogenetically.

PCR amplifi cation with degenerate oligonucleotide prim-ers (Clark et al., 1993; Schurmann et al., 1994) revealed the ex-istence of a large number of mammalian cDNAs encoding closely related proteins. The next to be cloned and sequenced were ARL2 (Clark et al., 1993), ARL3 (Cavenagh et al., 1994), ARL4 (Schurmann et al., 1994), and ARL5 (Breiner et al., 1996). Each of the encoded proteins has a glycine at position 2, the site of N-myristoylation in all Arf proteins. Note that although ARL2 and ARL3 have the NH2-terminal glycine, they appear not to be substrates for N-myristoyltransferases.

Around this time, a protein with similar percent identities to the Arf and Arls was found, but it lacked the NH2-terminal glycine, was membrane associated, and displayed distinctive nucleotide handling properties (Schurmann et al., 1995). Thus, it was given the name Arf-related protein 1 (ARFRP1) to distin-guish it from the Arls and Arfs. We realize today that this was unfortunate, as several of the more recently identifi ed Arls also have functions and biochemical properties that are quite diver-gent from Arfs.

SARs. SAR1 was among the earliest members of the Arf family sequenced, and it came out of genetic screens in the yeast S. cerevisiae as a suppressor of sec12(ts) (Nakano and Muramatsu, 1989). Its name is derived from its identifi cation as a secretion-associated and Ras-related protein. Cloning of the mammalian orthologues revealed the presence of two closely related (90% identity) proteins/genes (Kuge et al., 1994). With <30% identity to Arfs or Arls, the SAR proteins are only slightly closer in sequence to Arfs than to other families of GTPases, but they also share considerable functional relatedness to Arfs in that they act through the recruitment of coat proteins or complexes to initiate vesicle budding. SARs lack the other aforementioned Arf activities.

Addit ional domains. An interesting variation is found in ARD1/tripartite motif 23 (TRIM23), a 64-kD protein that possesses a ?20-kD domain at its COOH terminus with 60% identity to Arfs (Mishima et al., 1993). Originally named based on the presence of the Arf domain, ARD1 is also a member of the TRIM family, from which it obtained its current name, TRIM23.

A large extension is also seen in ARL13B, a protein of 428 res-idues that contains an Arl domain at its NH2 terminus (Chiang

et al., 2004; Fan et al., 2004). Although the NH2-terminal portion

of TRIM23 may possess GTPase-activating protein activity to-

ward its own Arf domain (Vitale et al., 1996) and E3 ubiquitin ligase activity (Vichi et al., 2005), the COOH-terminal portion of

ARL13B has no defi ned domains or functions to date.

De? ning the Arf family

As the discussion above suggests, there are no shared functions

or activities that justify grouping Arf, Arl, and SAR proteins

into a family with a common nomenclature. Similarities in pro-

tein sequences within the Arf family were fi rst identifi ed by alignment and phylogenetic analyses and were shown to pro-

vide distinct signatures that allowed differentiation from Ras,

G protein α subunits, and other GTPases. These include an NH2-terminal extension, a glycine acceptor for myristate at position 2,

an aspartate at position 26 (in contrast to the glycine 12 of Ras

that carries oncogenic potential), and other residues that are

very highly conserved within the family. These early observa-

tions were put on more solid functional footing when they were found to map to unique elements in their three-dimensional structures, which allow for the GDP/GTP switch to be coupled

with interaction signals opposite to the nucleotide-binding site (for review see Pasqualato et al., 2002). The prominent feature

of this unique nucleotide switch is a nonconventional GDP-bound form in which the two β strands that connect the n ucleotide-sensitive switch 1 and 2 regions (also called the interswitch) are retracted in the protein core and must undergo a two-residue

shift to reach the active conformation (Fig. 1). However, the in-terswitch cannot do so unless the NH2-terminal helical exten-sion, which caps the interswitch and locks it in the retracted conformation, has been displaced. In the case of ARF1, bio-chemical studies have established that this requires the interac-

tion of the NH2 terminus with membranes, thus allowing the nucleotide-binding site to detect and respond to remote protein–membrane interactions (Antonny et al., 1997). Like

Arf proteins, each Sar has an NH2-terminal amphipathic helix

that functions as a structural GDP/GTP switch to anchor the GTP-bound form to membranes of the endoplasmic reticulum (Huang et al., 2001; Bi et al., 2002). Furthermore, membrane insertion of this NH2-terminal helix was recently shown to initi-

ate membrane bending at the early stages of COPII coat assem-

bly and to be subsequently required for the completion of COPII vesicle fi ssion (Lee et al., 2005).

Structural analysis of ARF1 and ARF6 GDP/GTP cycles

and their comparison with those of small GTP-binding proteins whose interswitch does not toggle identifi ed three structural de-terminants for this movement: a helical NH2-terminal extension

that fastens the retracted, GDP-bound interswitch; a shorter in-terswitch that can retract completely; and a sequence signature (wDvGGqXXXRxxW) that provides both fl exibility for the movement (GG) and hydrogen bonds for stabilization of the ac-

tive conformation (R/W). These characteristics are p resent in all

Arf and most Arl sequences, which, therefore, are predicted to

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NOMENCLATURE FOR THE HUMAN A RF FAMILY ? KAHN ET AL.647

have the ability to undergo the interswitch toggle to detect inter-actions opposite to the nucleotide-binding site, whatever their nature, and propagate them to this site (Pasqualato et al., 2002).

These structural criteria for unifying Arf and Arl proteins as a family have since been supported by various structures of GDP-bound Arf and Arl proteins (Table S1, available at https://www.wendangku.net/doc/584043556.html,/cgi/content/full/jcb.200512057/DC1). It should be noted, however, that one subgroup, ARL4, has a long inter-switch that may have lost the ability to toggle, whereas struc-tures of NH 2-terminally truncated ARL8A and ARL8B bound to GDP have a GTP-like conformation. This suggests that trun-cation of the NH 2 terminus is suffi

cient in this family to destabi-lize the retracted interswitch or that these proteins have lost their ability to undergo the interswitch toggle. Recent work on ARL3 suggests that proteins interacting with the NH 2 terminus could also work as the displacing factor as an alternative to membranes (Behnia et al., 2004; Setty et al., 2004).

Arf family nomenclature

Table I contains information on proposed and previous names as well as other information on the human ARF family members. EST and genomic sequencing resulted in the identifi cation of subsequent Arf-like proteins, and these proteins/genes were of-ten misnamed or named multiple times by different research groups. Some of these names suggest relationships that are mis-leading, and some are called Arfs despite (presumably) lacking any Arf activities. In many cases, no functional data are yet available for the most recently identifi ed Arf family members. One protein has been referred to by four different names, and some proteins/genes were named by curators of databases re-sponding to specifi c requests in a manner that disagreed with common usage by researchers in the fi eld. The confusion is magnifi ed when species differences are considered (e.g., yeast Arl3 is the orthologue of ARFRP1).

The need for a generally agreed upon nomenclature for the ARF family has become acute as a result of increasing

c onfusion an

d interest in their study. It is not possibl

e today to propose a completely consistent nomenclature, as there are s imply

too many studies with some of the earlier discovered proteins (e.g., ARFRP1 should be an ARL).

The nomenclature developed and described in this article builds on previous efforts to describe phylogenetic relationships and bring consistency to nomenclature (Pasqualato et al., 2002; Li et al., 2004; Logsdon and K ahn, 2004). It is the result of many discussions between researchers in the fi eld and with the HUGO Genome Nomenclature Committee (HGNC) and has been widely circulated to Arf family researchers. We describe the presence in the human proteome of 29 members of the Arf family and a system for naming newly identifi ed proteins in hu-man or other species. The use of letter suffi xes is reserved for those groups of proteins within the family that share higher per-cent identities and are, therefore, likely to share some level of functional redundancy. One exception to this is the ARL13A and ARL13B proteins, which have been given a common num-ber based upon phylogenetic evidence. The consensus nomen-clature for the Arf family is shown in Table I along with previous names and unique gene/protein identifying information. Note that in three cases (ARL5C , ARL9, and ARL16), the intron/exon boundary predictions in the database are thought to be incorrect (based upon comparisons with sequences in other species), resulting in differences in the predicted protein sequences. In these cases, we use our corrected sequences for comparisons and provide the predicted protein sequences of the human pro-teins (see supplemental material, available at https://www.wendangku.net/doc/584043556.html,/cgi/content/full/jcb.200512057/DC1). In addition, there is one case (ARL9) in which it appears that alternative splicing yields two different proteins, one of which is truncated and pre-dicted to be unable to bind nucleotides, so both are provided in the supplemental protein sequence material.

We also identify several gene sequences that have ques-tionable EST/mRNA support and are likely pseudogenes derived from members of the Arf family. These genes, which are annotated by the HGNC, are therefore not included as Arf family members and are listed, along with their identifi

ers, in

Figure 1. The structural “air de famille.” In Arfs, Arls, and SAR proteins, the interswitch toggles from an unusual retracted conformation in the GDP-bound form that is fastened by the NH 2-terminal helix to an exposed conformation in the GTP-bound form that is stabilized by the W/GG/R signature (shown here for ARF6-GDP and ARF6-GTP). This large conforma-tional change, which involves a two-residue β-strand register shift in the core of the G domain, allows the nucleotide-binding site to detect remote interactions taking place at the NH 2 terminus (reproduced from Pasqualato et al., 2001 with permission).

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Table I. The Arf family GTPases: summary of names, identi? ers, and NH2-terminal sequences

Accepted symbols Proposed new names Previous

HGNC

symbol

Former

common

name

Other names

or information

Accession number

(protein)

Length

(aa)

NH2-terminal

sequence

Gene

locus

ID

Human

locus

ARF1ARF1ARF1NP_001649181M G N I F A N L F K G L 3751q42

ARF3ARF3ARF3NP_001650181M G N I F G N L L K S L 37712q13

ARF4ARF4ARF4NP_001651180M G L T I S S L F S R L 3783p21.2-p21.1 ARF5ARF5ARF5NP_001653180M G L T V S A L F S R I 3817q31.3

ARF6ARF6ARF6NP_001654175M G K V L S K I F G N K 38214q21.3 ARL1ARL1ARL1ARFL1NP_001168181M G G F F S S I F S S L 4007q13

ARL2ARL2ARL2ARFL2NP_001658184M G L L T I L K K M K Q 40211q13

ARL3ARL3ARL3ARFL3NP_004302182M G L L S I L R K L K S 40310q23.3 ARL4A b ADP ribosylation factorlike 4A ARL4c ARL4NP_005729200M G N G L S D Q T S I L 101247p21-p15.3 ARL4C b ADP ribosylation factorlike 4C ARL7c ARL7LAK NP_005728192M G N I S S N I S A F Q 101232q37.1

ARL4D b ADP ribosylation factorlike 4D ARF4L c ARL9ARL6/ARF4L/

ARL5/ARL4L

NP_001652201M G N H L T E M A P T A 37917q12-q21 ARL5A b ADP ribosylation factorlike 5A ARL5c ARL5NP_036229179M G I L F T R I W R L F 262252q23.3

ARL5B b ADP ribosylation factorlike 5B ARL8c ARL5B ARL8/similar to

ARL5/ARL5-like

NP_848930179M G L I F A K L W S L F 22107910p12.31 ARL5C b ADP ribosylation factorlike 5C ARL12c ARL12XP_372668179a M G Q L I A K L M S I F 39079017q12

ARL6ARL6ARL6BBS3NP_115522186M G L L D R L S V L L G 841003q11.2

ARL8A b ADP ribosylation factorlike 8A ARL10B c ARL8A ARL10B/GIE2NP_620150186M I A L F N K L L D W F 1278291q32.1

ARL8B b ADP ribosylation factorlike 8B ARL10C c ARL8B ARL10C/GIE1NP_060654186M L A L I S R L L D W F 552073p26.1

ARL9ARL9NP_996802123/

265a M E F L E I G G S K/

M E R G K V K K K E

1329464q12

ARL10b ADP ribosylation factorlike 10ARL10A c ARL10A NP_775935244M A P R P L G P L V L A 2855985q35.2

ARL11ARL11ARL11ARLTS1NP_612459196M G S V N S R G H K A E 11576113q14.2

ARL13A b ADP ribosylation factorlike 13A ARL13c dJ341D10.2NP_001013008297M F R L L S S C C S C L 392509Xq22.1

ARL13B b ADP ribosylation factorlike 13B ARL2L1c DKFZp761H079NP_878899428M F S L M A S C C G W F 2008943q11.2

ARL14b ADP ribosylation factorlike 14ARF7c ARL10ARF7NP_079323192M G S L G S K N P Q T K 801173q25.33

ARL15b ADP ribosylation factorlike 15ARFRP2c FLJ20051NP_061960204M S D L R I T E A F L Y 546225p15.2

ARL16b ADP ribosylation factorlike 16LOC339231XP_290777173a M C L L L G A T G V G K 33923117q25.3 ARFRP1ARFRP1ARFRP1Arp, Arp1NP_003215201M Y T L L S G L Y K Y M 1013920q13.3

SAR1A b SARA1c SAR1A HsSara1NP_064535198M S F I F E W I Y N G F 5668110q22.1

SAR1B b SARA2c SAR1B HsSara2NP_057187198M S F I F D W I Y S G F 511285q31.1

TRIM23TRIM23ARD1 (α)ARFD1, RNF46NP_001647574M A T L W N K L G A G 3735q12.3

Because of previous usage and to avoid confusion, the new assignments result in there being no gene/protein named ARL7 or ARL12. See Table S2 for a list of earlier names and references in which earlier names were used (available at https://www.wendangku.net/doc/584043556.html,/cgi/content/full/jcb.200512057/DC1).

a The sequence currently in the database is predicted to be incorrect, and our corrected information was used herein.

b New names approved by the HGNC.

c Previous names that were recently changed.

Table II. It is expected that additional pseudogenes will be found and added to this list over time. We also note some uncer-tainty as to whether ARL5C in Table I is a transcribed gene, as it may lack part of the consensus GTP-binding signature d epending on which predicted protein sequence is used.

Finally, we note that although the large majority of Arf family members appear to have very broad and perhaps ubiqui-tous tissue expression patterns, a few are far more restricted in their expression. Thus, it is expected that further additions and perhaps even deletions will be needed to keep the nomenclature of this family current and as consistent as possible. To ensure that new family members are assigned unique symbols, we strongly encourage authors to consult the HGNC before pub-lishing any new names for members of this gene/protein family. This is a confi dential service provided by the HGNC that will help prevent future confusion from arising. We also suggest that curators and researchers focusing on other organisms use the information provided in this article as much as possible to sim-plify and clarify the nomenclature across species.

Other researchers supporting the use of this nomencla-

ture include: Bruno Antonny, Bill Balch, Vytas Bankaitis, Gary Bokoch, Juan Bonifacino, Chris Burd, Jim Casanova, Tamara Caspary, Dany Cassel, Rick Cerione, Pierre Chardin, Philippe Chavrier, Shamshad Cockcroft, Peter Cullen, Ivan

de Curtis, Maria Antonella De Matteis, Julie Donaldson, Cryslin D’ S ouza-Schorey, John Exton, Victor Faundez, Jim Goldenring, Jean Gruenberg, Alan Hall, Fuchu He, Wangjin Hong, Victor Hsu, Mary Hunzicker-Dunn, Trevor Jackson, Cathy Jackson, Hans Joost, Toshi K atada, Fang-jen Lee, Michel Leroux, Jennifer Lippincott-Schwartz, John Logsdon, Alberto Luini, Vivek Malhotra, Ed Manser, Tobias Meyer, Paul Melancon, Joel Moss, Aki Nakano, Kazu Nakayama, Tommy Nilsson, Susanne Pfeffer, Richard Premont, Paul Randazzo, Anne Ridley, Scotty Robinson, Anne Rosenwald, Craig Roy, Hisataka Sabe, Randy Schekman, Nava Segev, Val Sheffi eld,

Phil Stahl, Elizabeth Sztul, Chris Turner, Anne Theibert, Martha Vaughan, K anamarlapudi Venkateswarlu, Fred Wittinghofer, Keqiang Ye, and Marino Zerial.

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This work was supported by grants from the National Institutes of Health (GM68029 and GM67226 to R.A. Kahn), the Association pour la Recerche contre la Cancer (to J. Cher? ls), and the French Research Ministry (ACI-BCMS to J. Cher? ls).

Submitted: 9 December 2005Accepted: 24 January 2006

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Table II. Pseudogenes of the Arf family in the human genome

New symbol New name

Other names/information

Chromosome location Accession number Gene locus

ID ARF1P1ADP ribosylation factor 1 pseudogene 17q21.3XM_498225442334ARF1P2ADP ribosylation factor 1 pseudogene 2ARL17A 17q21.31NM_016632.151326ARF4P ADP ribosylation factor 4 pseudogene 9q34NG_001075380ARF4P2ADP ribosylation factor 4 pseudogene 220q13.33NG_001031170485ARF4P3ADP ribosylation factor 4 pseudogene 313q32.3XM_372496390423ARL4P ADP ribosylation factorlike 4 pseudogene ARL4B 10q21.2XM_370560387684ARL4P2ADP ribosylation factorlike 4 pseudogene 2ARL4B 4p14NG_005394152709SAR1P1SAR1 gene homologue (S. cerevisiae ) pseudogene 1SARAP 6p21AL0354********SAR1P2SAR1 gene homologue (S. cerevisiae ) pseudogene 2SARA1P 10q26.2AC026226641312SAR1P3

SAR1 gene homologue (S. cerevisiae ) pseudogene 3

4q27

XP_293671

344988

This is a list of the HGNC-recognized pseudogenes from the Arf family along with their locations in the genome, accession numbers, and gene identi? ers.

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Sewell, J.L., and R.A. K ahn. 1988. Sequences of the bovine and yeast ADP-

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J.A. Kennison. 1991. The arfl ike gene encodes an essential GTP-binding protein in Drosophila . Proc. Natl. Acad. Sci. USA . 88:3120–3124.

Tsuchiya, M., S.R. Price, S.C. Tsai, J. Moss, and M. Vaughan. 1991. Molecular

identifi cation of ADP-ribosylation factor mRNAs and their expression in mammalian cells. J. Biol. Chem. 266:2772–2777.

Vichi, A., D.M. Payne, G. Pacheco-Rodriguez, J. Moss, and M. Vaughan. 2005.

E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1). Proc. Natl. Acad. Sci. USA . 102:1945–1950.Vitale, N., J. Moss, and M. Vaughan. 1996. ARD1, a 64-kDa bifunctional pro-tein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain. Proc. Natl. Acad. Sci. USA . 93:1941–1944.

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