Adenosine 5′-0(3-thiotriphosphate) in the control of phosphorytase activity

Gratecos, D.; Fischer, Edmond H.

doi:10.1016/s0006-291x(74)80237-8

Cited by 195 publications

(85 citation statements)

References 21 publications

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“…These analogs have been shown to act as inhibitors and substrates of nucleotide-dependent systems, in particular the phosphatases [20,21]. ATP[yS] has also been shown to inhibit the myosin ATPase in muscle, causing relaxation of the muscle but not contraction [22,23]. These compounds would be expected to bind to the substrate binding sites of their respective phosphohydrolases with an affinity similar to that of the substrate.…”

Section: Discussionmentioning

confidence: 99%

Comparison of effects of inhibitors on adenosine triphosphatase and adenosine diphosphatase activities in rat‐liver mitochondria

Montague

Baum

1984

European Journal of Biochemistry

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Adenosine diphosphatase (ADPase) activity and ATPase activity were assayed in rat liver mitochondria and outer mitochondrial membrane preparations with [P-32P]ADP and [Y-~~P]ATP as substrates. Inhibition studies were performed with the mitochondrial ATPase inhibitor oligomycin and the adenine nucleotide transport inhibitor, carboxyatractyloside. Kinetic studies were also performed with the nucleotide thiophosphate analogs adenosine 5'-0-thiophosphate, adenosine 5'-0-(2-thiodiphosphate) and adenosine 5'-0-(3-thiotriphosphate) which can act as inhibitors of phosphohydrolases. It is concluded that part of the apparent ADPase activity of intact mitochondria is mediated via ATPase, presumably in conjunction with adenylate kinase. In addition the outer mitochondrial membrane appears to show a distinct ADPase not attributable to contamination by inner membrane ATPase.Adenosine diphosphatase activity has been shown to be associated with vascular cells [1 -31, plasma [4], cultured arterial and smooth muscle cells [5,6], heart [7] and lung [8]. Rat liver has also been shown to possess an ADPase activity [9]. Analytical subcellular fractionation of rat liver in a zonal rotor showed that ADPase had the same unimodal distribution profile as the mitochondrial marker succinate dehydrogenase. 5'-Nucleotidase, a plasma membrane marker, had a different modal density from ADPase and was clearly separated. N-Acetyl-P-glucosaminidase, a lysosomal marker, and neutral a-glucosidase, an endoplasmic reticulum marker, had similar modal densities, but different distribution profiles, to that of ADPase. In addition, experiments performed with the perturbants Triton WR1339 and pyrophosphate showed clearly that ADPase was located in a different cellular compartment to these two markers [9]. Further subcellular fractionation, by digitonin treatment, showed that the activity was localised in the outer mitochondrial membrane. However, 15 % of the mitochondrial ATPase, which exhibits about ten times the phosphohydrolase activity associated with ADPase, was also found in the outer mitochondrial membrane fraction. One can therefore ask whether the ADPase activity associated with the outer mitochondrial membrane is distinct or merely reflects the ATPase activity of this fraction.The present study utilised the inhibitors carboxyatractyloside and oligomycin and the adenosine thiophosphate analogs of AMP, ADP and ATP to attempt to answer this question.

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Section: Discussionmentioning

confidence: 99%

Comparison of effects of inhibitors on adenosine triphosphatase and adenosine diphosphatase activities in rat‐liver mitochondria

Montague

Baum

1984

European Journal of Biochemistry

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“…Higher nonhydrolyzable nucleotide analog concentrations or longer incubation times did not restore the coating activity (data not shown). Since ATP␥S can substitute for ATP as a substrate for protein kinases (Gratecos and Fischer, 1974;Nichols et al, 1990), these results suggest that a phosphorylation reaction is required for the AP-3 coat recruitment to synaptic vesicles. …”

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confidence: 90%

The AP-3 Complex Required for Endosomal Synaptic Vesicle Biogenesis is Associated with a Casein Kinase Ια-Like Isoform

Faúndez

Kelly

2000

MBoC

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The formation of small vesicles is mediated by cytoplasmic coats the assembly of which is regulated by the activity of GTPases, kinases, and phosphatases. A heterotetrameric AP-3 adaptor complex has been implicated in the formation of synaptic vesicles from PC12 endosomes . When the small GTPase ARF1 is prevented from hydrolyzing GTP, we can reconstitute AP-3 recruitment to synaptic vesicle membranes in an assembly reaction that requires temperatures above 15°C and the presence of ATP suggesting that an enzymatic step is involved in the coat assembly. We have now found an enzymatic reaction, the phosphorylation of the AP-3 adaptor complex, that is linked with synaptic vesicle coating. Phosphorylation occurs in the ␤3 subunit of the complex by a kinase similar to casein kinase 1␣. The kinase copurifies with neuronal-specific AP-3. In vitro, purified casein kinase I selectively phosphorylates the ␤3A and ␤3B subunit at its hinge domain. Inhibiting the kinase hinders the recruitment of AP-3 to synaptic vesicles. The same inhibitors that prevent coat assembly in vitro also inhibit the formation of synaptic vesicles in PC12 cells. The data suggest, therefore, that the mechanism of AP-3-mediated vesiculation from neuroendocrine endosomes requires the phosphorylation of the adaptor complex at a step during or after AP-3 recruitment to membranes. INTRODUCTIONMembrane proteins are carried from donor membranes to acceptor membranes by two steps, the vesiculation of a carrier vesicle from the donor and the fusion of the carrier vesicle with the acceptor. Vesiculation of the donor membrane can itself be divided into five steps: recognition of cargo proteins; recruitment of coating molecules; the imposition of curvature on the forming vesicle membrane; fission of the carrier vesicle from the donor membrane; and, finally, the loss of the vesicle coat (Springer et al., 1999). To discover the molecular events that take place at each step, several laboratories have reconstituted either the entire process of vesiculation or individual steps in vitro.The first two steps of vesiculation, cargo recognition and coating, can be regulated by phosphorylation. Membrane proteins are recognized as cargo because they contain sorting domains. Adaptors interact with a tyrosine or a dileucine motif (Schmid, 1997;Kirchhausen et al., 1997;Bonifacino and Dell'Angelica, 1999). The recognition of cargo molecules can be regulated by the phosphorylation of sites close to the sorting domains; for example, in the trafficking of furin (Wan et al., 1998;Teuchert et al., 1999;Molloy et al., 1999), CD4 (Pitcher et al., 1999), CTLA-4 (Shiratori et al., 1997), MHC-II-Ii complex (Anderson and Roche, 1998), and pIgAR (Casanova et al., 1990;Okamoto et al., 1994;Luton et al., 1998). The cargo molecules are recruited into a newly forming carrier vesicle by cytoplasmic coat molecules (Matsuoka et al., 1998;Bremser et al., 1999). The recruitment of two of the known coats, COPI and COPII, is regulated by small ARF-like GTPases and appears to be a relatively simple p...

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“…This ATP analog can be used by protein kinases to phosphorylate proteins, but the dephosphorylation of the resultant phosphoproteins by protein phosphatases is greatly inhibited (Gratecos and Fisher, 1974). Therefore, ATPyS acts as a phosphatase inhibitor or antagonist.…”

Section: The Ik0 In Mesophyll Cells 1s Enhanced By Protein Phosphatasmentioning

confidence: 99%

Evidence for Protein Phosphatase 1 and 2A Regulation of K+ Channels in Two Types of Leaf Cells

Luan

Schreiber

et al. 1994

Plant Physiol.

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an inward rectifying channel that is activated upon membrane hyperpolarization and an outward rectifying channel that is activated by depolarization of the membrane (Schroeder, 1988; Hedrich and Schroeder, 1989). Recent studies have begun to distinguish the components of signal transduction pathways that regulate various responses. Guard cells in particular have been used as a model system to study the regulation of K+ channels, and thus stomatal aperture, by

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Adenosine 5′-0(3-thiotriphosphate) in the control of phosphorytase activity

Cited by 195 publications

References 21 publications

Comparison of effects of inhibitors on adenosine triphosphatase and adenosine diphosphatase activities in rat‐liver mitochondria

Comparison of effects of inhibitors on adenosine triphosphatase and adenosine diphosphatase activities in rat‐liver mitochondria

The AP-3 Complex Required for Endosomal Synaptic Vesicle Biogenesis is Associated with a Casein Kinase Ια-Like Isoform

Evidence for Protein Phosphatase 1 and 2A Regulation of K+ Channels in Two Types of Leaf Cells

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