Characterization of a Fourth Adaptor-related Protein Complex

Hirst, Jennifer; Bright, Nicholas A.; Rous, Brian; Robinson, Margaret S.

doi:10.1091/mbc.10.8.2787

Cited by 292 publications

(297 citation statements)

References 49 publications

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“…Although the most intensively studied aspect of BFA action is the ARFdependent recruitment of COP-I to Golgi membranes, it is also known that BFA induces alterations in the localization of markers of the TGN, specifically M6PR, resulting in increased staining at the plasma membrane. The recruitment of other coat complexes, specifically AP-1 (Stamnes and Rothman, 1993;Traub et al, 1993), AP-3 (Simpson et al, 1997;Faundez et al, 1998;Ooi et al, 1998), andAP-4 (Dell'Angelica et al, 1999;Hirst et al, 1999), has also been shown to be BFA sensitive and, thus, predicted to require active ARF.…”

Section: Discussionmentioning

confidence: 99%

“…Results from several laboratories have pointed to a central role for ARFs in regulating some aspect of membrane traffic, particularly to and from the Golgi, and more recently from the trans-Golgi network (TGN) (Stamnes and Rothman, 1993;Traub et al, 1993;Ooi et al, 1998;Hirst et al, 1999). ARFs were originally found to localize to the Golgi (Stearns et al, 1990b).…”

Section: Introductionmentioning

confidence: 99%

“…AP-2 associates with plasma membranes in an ARFsensitive manner (West et al, 1997) and is found on endosomes derived from the plasma membrane. AP-3 (Dell'Angelica et al, 1997;Simpson et al, 1997;Ooi et al, 1998) and AP-4 (Dell'Angelica et al, 1999;Hirst et al, 1999) are involved in transport within the endosomal-lysosomal system and in the transport of non-clathrin-coated vesicles from the TGN, respectively.…”

Section: Introductionmentioning

confidence: 99%

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A Family of ADP-Ribosylation Factor Effectors That Can Alter Membrane Transport through thetrans-Golgi

Boman

Zhang

Zhu

et al. 2000

MBoC

264

247

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A family of three structurally related proteins were cloned from human cDNA libraries by their ability to interact preferentially with the activated form of human ADP-ribosylation factor 3 (ARF3) in two-hybrid assays. The specific and GTP-dependent binding was later confirmed through direct protein binding of recombinant proteins. The three proteins share large (Ϸ300 residues) domains at their N termini that are 60 -70% identical to each other and a shorter (73 residues) domain at their C termini with 70% homology to the C-terminal "ear" domain of ␥-adaptin. Although GGA1 is found predominantly as a soluble protein by cell fractionation, all three proteins were found to localize to the trans-Golgi network (TGN) by indirect immunofluorescence. The binding of GGAs to TGN was sensitive to brefeldin A, consistent with this being an ARF-dependent event. Thus, these proteins have been named Golgi-localizing, ␥-adaptin ear homology domain, ARF-binding proteins, or GGAs. The finding that overexpression of GGAs was sufficient to alter the distribution of markers of the TGN (TGN38 and mannose 6-phosphate receptors) led us to propose that GGAs are effectors for ARFs that function in the regulation of membrane traffic through the TGN.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A Family of ADP-Ribosylation Factor Effectors That Can Alter Membrane Transport through thetrans-Golgi

Boman

Zhang

Zhu

et al. 2000

MBoC

264

247

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“…The best-studied function of Arfs is in the formation of COPI-coated vesicles from the Golgi (reviewed in Wieland and Harter, 1999). Arfs have also been implicated in the formation of a number of different vesicle coats and in many different steps in secretion (Balch et al, 1992;Boman et al, 1992;Lenhard et al, 1992;Stamnes and Rothman, 1993;Traub et al, 1993;Letourneur et al, 1994;West et al, 1997;Ooi et al, 1998;Hirst et al, 1999). Indeed, mutations of ARF1 in yeast result in pleiotropic defects in the processing of secreted proteins, as well as aberrant morphology of intracellular organelles (Stearns et al, 1990b;Gaynor et al, 1998;Yahara et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Systematic Structure-Function Analysis of the Small GTPase Arf1 in Yeast

Click¹,

Stearns

Botstein³

2002

MBoC

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Members of the ADP-ribosylation factor (Arf) family of small GTPases are implicated in vesicle traffic in the secretory pathway, although their precise function remains unclear. We generated a series of 23 clustered charge-to-alanine mutations in the Arf1 protein ofSaccharomyces cerevisiae to determine the portions of this protein important for its function in cells. These mutants display a number of phenotypes, including conditional lethality at high or low temperature, defects in glycosylation of invertase, dominant lethality, fluoride sensitivity, and synthetic lethality with thearf2 null mutation. All mutations were mapped onto the available crystal structures for Arf1p: Arf1p bound to GDP, to GTP, and complexed with the regulatory proteins ArfGEF and ArfGAP. From this systematic structure-function analysis we demonstrate that all essential mutations studied map to one hemisphere of the protein and provide strong evidence in support of the proposed ArfGEF contact site on Arf1p but minimal evidence in support of the proposed ArfGAP-binding site. In addition, we describe the isolation of a spatially distant intragenic suppressor of a dominant lethal mutation in the guanine nucleotide-binding region of Arf1p.

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“…However, AP-3 does not associate with clathrin (19 -22). Yet another recently described adaptor protein, AP-4, has no known function (24,25).…”

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confidence: 99%

The Vesicular Acetylcholine Transporter Interacts with Clathrin-associated Adaptor Complexes AP-1 and AP-2

Kim

Hersh

2004

Journal of Biological Chemistry

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In neuronal cells the neurotransmitter acetylcholine is transferred from the cytoplasm into synaptic vesicles by the vesicular acetylcholine transporter (VAChT). The cytoplasmic tail of VAChT has been shown to contain signals that direct its sorting and trafficking. The role of clathrin-associated protein complexes in VAChT sorting to synaptic vesicles has been examined. A fusion protein between the VAChT cytoplasmic tail and glutathione S-transferase was used to identify VAChT-clathrin-associated protein adaptor protein 1, adaptor protein 2 and adaptor protein 180 complexes from a rat brain extract. In vivo coimmunoprecipitation confirmed adaptin ␣ and adaptin ␥ complexes, but adaptor protein 180 complexes were not detected by this technique. Deletion and site directed mutagenesis show that the VAChT cytoplasmic tail contains multiple trafficking signals. These include a non-classical tyrosine motif that serves as the signal for adaptin ␣ and a dileucine motif that serves as the signal for adaptin ␥. A classical tyrosine motif is also involved in VAChT trafficking, but does not interact with any known adaptor proteins. There appear to be two endocytosis motifs, one involving the adaptor protein 1 binding site and the other involving the adaptor protein 2 binding site. These results suggest a complex trafficking pathway for VAChT.

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Characterization of a Fourth Adaptor-related Protein Complex

Cited by 292 publications

References 49 publications

A Family of ADP-Ribosylation Factor Effectors That Can Alter Membrane Transport through thetrans-Golgi

A Family of ADP-Ribosylation Factor Effectors That Can Alter Membrane Transport through thetrans-Golgi

Systematic Structure-Function Analysis of the Small GTPase Arf1 in Yeast

The Vesicular Acetylcholine Transporter Interacts with Clathrin-associated Adaptor Complexes AP-1 and AP-2

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