Arfaptin 1 forms a complex with ADP‐ribosylation factor and inhibits phospholipase D

Williger, Ben-Tsion; Provost, Joseph; Ho, Wan Ting; Milstine, J; Exton, John H.

doi:10.1016/s0014-5793(99)00771-1

Cited by 24 publications

(19 citation statements)

References 17 publications

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“…However, the inclusion of POR1⌬N in the pre-activation step of ARF3 with GTP␥S almost completely eliminated this increase in PLD activity. These data indicate that PLD1 and POR1 cannot simultaneously bind productively to ARF3, as previously reported (47). Although this may appear to suggest that the activated ARF is not free to dissociate in the active state and to interact with other effectors, such a conclusion cannot be drawn until we know more about the binding constants of active ARF for the different effectors and the relative abundance of each.…”

Section: Table II Por1 Binding Of Arf3 Prevents Activation Of Pld1supporting

confidence: 68%

Effectors Increase the Affinity of ADP-ribosylation Factor for GTP to Increase Binding

Zhu

Boman²,

Kuai

et al. 2000

Journal of Biological Chemistry

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The stoichiometry of the binding of GTP to ADP-ribosylation factor (ARF) proteins, normally quite low at ϳ0.05 mol/mol protein, was found to increase to a maximum of 1 mol/mol in the presence of effectors. The mechanism of this action was found to result from the ability of these effectors to increase the affinity of ARF for activating guanine nucleotide triphosphates. The existence of a conformation of ARF with low affinity (>100 M) for GTP is proposed. The actions of effectors to increase the equilibrium binding of GTP is interpreted as evidence that these same effectors interact with and modulate the affinity of the inactive ARF for GTP. A new model for these interactions among ARF, effectors, and GTP is proposed, and a preliminary test in cells is supportive of these observations with relevance to signaling in cells.

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Section: Table II Por1 Binding Of Arf3 Prevents Activation Of Pld1supporting

confidence: 68%

Effectors Increase the Affinity of ADP-ribosylation Factor for GTP to Increase Binding

Zhu

Boman²,

Kuai

et al. 2000

Journal of Biological Chemistry

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“…Arfaptin 1 and 2 are cytosolic proteins that bind small GTPases of the ARF family (8) and Rac1 (7). Arfaptin 1, in particular, is recruited to Golgi membranes by ARF1-GTP and acts as negative regulator of ARF1 function (8,58,59). Arfaptin is composed of three ␣-helices that dimerize to form the binding interface for small GTPases.…”

Section: Enrichment Of Ica69 On the Golgi Complex By Subcellularmentioning

confidence: 99%

Islet Cell Autoantigen of 69 kDa Is an Arfaptin-related Protein Associated with the Golgi Complex of Insulinoma INS-1 Cells

Spitzenberger

Pietropaolo

Verkade

et al. 2003

Journal of Biological Chemistry

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Islet cell autoantigen of 69 kDa (ICA69) is a cytosolic protein of still unknown function. Involvement of ICA69 in neurosecretion has been suggested by the impairment of acetylcholine release at neuromuscular junctions upon mutation of its homologue gene ric-19 in C. elegans. In this study, we have further investigated the localization of ICA69 in neurons and insulinoma INS-1 cells. ICA69 was enriched in the perinuclear region, whereas it did not co-localize with markers of synaptic vesicles/synaptic-like microvesicles. Confocal microscopy and subcellular fractionation in INS-1 cells showed co-localization of ICA69 with markers of the Golgi complex and, to a minor extent, with immature insulin-containing secretory granules. The association of ICA69 with these organelles was confirmed by immunoelectron microscopy. Virtually no ICA69 immunogold labeling was observed on secretory granules near the plasma membrane, suggesting that ICA69 dissociates from secretory granule membranes during their maturation. In silico sequence and structural analyses revealed that the N-terminal region of ICA69 is similar to the region of arfaptins that interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. ICA69 is therefore a novel arfaptin-related protein that is likely to play a role in membrane trafficking at the Golgi complex and immature secretory granules in neurosecretory cells.

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“…Arfaptin-1 interacts with Arf1, Arf3, Arf5, and Arf6 (5, 7), localizes to the Golgi apparatus (5), and inhibits phospholipase D (12,13). On the other hand, arfaptin-2/POR1 interacts with all Arf proteins examined (14,15) and an Arf-like protein, Arl1 (15,16), regulates cytoskeletal rearrangements at the cell periphery induced by Arf6 and Rac1 (6), and modifies aggregation of polyglutamine-expanded huntingtin (17,18).…”

mentioning

confidence: 99%

Arfaptins Are Localized to the trans-Golgi by Interaction with Arl1, but Not Arfs

Man

Kondo

Koga

et al. 2011

Journal of Biological Chemistry

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Arfaptin 1 forms a complex with ADP‐ribosylation factor and inhibits phospholipase D

Cited by 24 publications

References 17 publications

Effectors Increase the Affinity of ADP-ribosylation Factor for GTP to Increase Binding

Effectors Increase the Affinity of ADP-ribosylation Factor for GTP to Increase Binding

Islet Cell Autoantigen of 69 kDa Is an Arfaptin-related Protein Associated with the Golgi Complex of Insulinoma INS-1 Cells

Arfaptins Are Localized to the trans-Golgi by Interaction with Arl1, but Not Arfs

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