The KDEL Receptor Regulates a GTPase-activating Protein for ADP-ribosylation Factor 1 by Interacting with Its Non-catalytic Domain

Aoe, Tomohiko; Huber, Irit; Vasudevan, Chandrasekaran; Watkins, Simon C.; Romero, Guillermo; Cassel, Dan; Hsu, Victor

doi:10.1074/jbc.274.29.20545

Cited by 40 publications

(28 citation statements)

References 40 publications

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“…At this time, it remains unclear whether this is achieved by multiple distinct ARF-GAP activities, by proteins regulating ARF-GAP activity, or by a combination of both mechanisms. In this context, it will be interesting to analyze the functional relevance of ARF-GAP interactions with SNAREs (43) and the KDEL receptor (44,45). …”

Section: Discussionmentioning

confidence: 99%

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

Reinhard

Schweikert

Wieland

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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Coat protein I (COPI)-coated transport vesicles mediate protein and lipid transport in the early secretory pathway. The basic machinery required for the formation of these transport intermediates has been elucidated based on the reconstitution of COPI-coated vesicle formation from chemically defined liposomes. In this experimental system, the coat components coatomer and GTP-bound ADPribosylation factor (ARF), as well as p23 as a membrane-bound receptor for COPI coat proteins, were shown to be both necessary and sufficient to promote COPI-coated vesicle formation. coatomer ͉ ADP-ribosylation factor ͉ ARF-GAP ͉ p24 protein family

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Section: Discussionmentioning

confidence: 99%

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

Reinhard

Schweikert

Wieland

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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“…By contrast, the similarity between Glo3p and Gcs1p is very low in other regions of the molecules. It has also been reported that the C-terminal non-catalytic domain of rat Arfgap1 is required for its recruitment from cytoplasm to membranes and for its interaction with the KDEL receptor (Aoe et al, 1999;Huber et al, 1998). From these aspects, we suspected that the clue to understand the difference between Glo3p and Gcs1p in vivo lies in the C-terminal domains of the proteins.…”

Section: Glo3 Is a Multicopy Suppressor Of Arf1-16 And Arf1-17mentioning

confidence: 92%

The Arf1p GTPase-activating protein Glo3p executes its regulatory function through a conserved repeat motif at its C-terminus

Yahara

Sato

Nakano

2006

Journal of Cell Science

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ADP-ribosylation factors (Arfs), key regulators of intracellular membrane traffic, are known to exert multiple roles in vesicular transport. We previously isolated eight temperature-sensitive (ts) mutants of the yeast ARF1 gene, which showed allele-specific defects in protein transport, and classified them into three groups of intragenic complementation. In this study, we show that the overexpression of Glo3p, one of the GTPase-activating proteins of Arf1p (ArfGAP), suppresses the ts growth of a particular group of the arf1 mutants (arf1-16 and arf1-17). Other ArfGAPs do not show such a suppression activity. All these ArfGAPs show sequence similarity in the ArfGAP catalytic domain, but are divergent in the rest of molecules. By domain swapping analysis of Glo3p and another ArfGAP, Gcs1p, we have shown that the non-catalytic Cterminal region of Glo3p is required for the suppression of the growth defect in the arf1 ts mutants. Interestingly, Glo3p and its homologues from other eukaryotes harbor a well-conserved repeated ISSxxxFG sequence near the Cterminus, which is not found in Gcs1p and its homologues. We name this region the Glo3 motif and present evidence that the motif is required for the function of Glo3p in vivo.Supplementary material available online at

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“…The non-catalytic part mediates the interaction of ArfGAP1 with loosely packed lipids (24) and is also involved in protein-protein interactions, as demonstrated for the interaction of ArfGAP1 with the COPI cargo, the KDEL receptor (29,30). However, a role of any of these interactions in the Golgi localization of ArfGAP1 has not been established.…”

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confidence: 99%

Golgi Localization Determinants in ArfGAP1 and in New Tissue-specific ArfGAP1 Isoforms

Parnis

Rawet

Regev

et al. 2006

Journal of Biological Chemistry

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The Arf1-directed GTPase-activating protein ArfGAP1 is a Golgi-localized protein that controls the dynamics of the COPI coat of carriers that mediate transport in the endoplasmic reticulumGolgi shuttle. Previously the interaction of ArfGAP1 with the Golgi was allocated to a portion of the non-catalytic, carboxyl part of the protein, but the mechanism of this interaction has not been established. In this study we identify a short stretch in the non-catalytic part of ArfGAP1 (residues 204 -214) in which several hydrophobic residues contribute to Golgi localization. Even single alanine replacement of two of these residues (Leu-207 and Trp-211) strongly diminished Golgi localization. Mutations in the hydrophobic residues also diminished the in vitro activity of ArfGAP1 on Arf1 bound to Golgi membranes. The stretch containing the hydrophobic residues was recently shown to mediate the binding of ArfGAP1 to loosely packed lipids of highly curved liposomes (Bigay, J., Casella, J. F., Drin, G., Mesmin, B., and Antonny, B. (2005) EMBO J. 24, 2244 -2253). Whereas short fragments containing the hydrophobic stretch were not Golgi-localized, a proximal 10-residue inframe insertion that is present in new ArfGAP1 isoforms that we identified in brain and heart tissues could confer Golgi localization on these fragments. This localization was abrogated by alanine replacement of residues Phe-240 or Trp-241 of the insertion sequence but not by their replacement with leucines. Our findings indicate that ArfGAP1 interacts with the Golgi through multiple hydrophobic motifs and that alternative modes of interaction may exist in tissue-specific ArfGAP1 isoforms.Membrane traffic in the endoplasmic reticulum-Golgi shuttle is mediated by the COPI 3 and COPII trafficking systems. The COPII system mediates the initial exit from the endoplasmic reticulum, whereas subsequent transport to the Golgi apparatus and retrograde Golgi to endoplasmic reticulum traffic involves COPI carriers. The COPI and COPII coats are composed of evolutionarily distinct sets of proteins yet follow similar pathways of coat assembly and disassembly (for recent reviews see Refs. 1-3). In both systems a small GTPase (Arf1 and Sar1 for COPI and COPII, respectively) plays a key regulatory role. Following activation by a guanine nucleotide exchange protein, the GTPase translocates from cytosol to the organelle membrane, where it initiates the process of coat formation by the direct binding of coat subunits (4 -6). The coat in turn recruits cargo and polymerizes causing membrane deformation to form a bud.In the second phase of the GTPase cycle of Arf1 and Sar1, bound GTP is hydrolyzed with the aid of a GTPase-activating protein (GAP). The hydrolysis of GTP is a prerequisite for coat dissociation, and its inhibition leads to the accumulation of coated vesicles that are prevented from fusing with the target membrane (4, 7). The GAP for Sar1 is a subunit of the first layer of the COPII coat, the Sec23/24 complex (8). ArfGAPs constitute a large family of proteins containing a hi...

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The KDEL Receptor Regulates a GTPase-activating Protein for ADP-ribosylation Factor 1 by Interacting with Its Non-catalytic Domain

Cited by 40 publications

References 40 publications

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

Functional reconstitution of COPI coat assembly and disassembly using chemically defined components

The Arf1p GTPase-activating protein Glo3p executes its regulatory function through a conserved repeat motif at its C-terminus

Golgi Localization Determinants in ArfGAP1 and in New Tissue-specific ArfGAP1 Isoforms

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