Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A protein fraction from the cellular slime mold Dictyostelium discoideum confers Ca2+-sensitivity on the activation of purified myosin adenosinetriphosphatase (ATP phosphohydrolase, EC 3.6.1.3) from Dictyostelium by purified Dictyostelium actin. That is, the fraction inhibits the actomyosin adenosine triphosphatase activity in the absence of Ca+ but not in the presence of Ca2+. This Ca2+-sensitizing factor affects only the actin-activated myosin adenosine triphosphatase and not the enzyme activity of myosin alone. The Ca2+-sensitivity is conserved when muscle actin replaces Dictyostelium actin, but is lost when muscle myosin replaces Dictyostelium myosin. The factor appears to be a protein since it is nondialyzable, is heat labile, and can be precipitated with ammonium sulfate. The factor can be purified 70-fold on an actin-affinity column.
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PMID:Calcium control of actin-activated myosin adenosine triphosphatase from Dictyostelium discoideum. 13 52

Analysis of the respiratory chain of spores of Dictyostelium discoideum, which lack a cyanide-sensitive respiration, indicated that cytochromes a-a3, b, and c-c1 are present at levels identical to those found in the vegetative amoebae. The specific activities of enzymes of both the respiratory chain and the citric acid cycle in the 600 x g supernatant fraction of sonically treated spores were at least as high as in similar preparations of amoebae. The activities of glutamic dehydrogenase and oligomycin-sensitive adenosine triphosphatase were reduced in the spores 30 and 56%, respectively. Intact spores appeared to lack a cyanide-sensitive respiration as a result of inadequate quantities of respiratory substrate and, more importantly, as a result of a lack of the cofactor nicotinamide adenine dinucleotide. The emergence phase of spore germination was sensitive to the antibiotic chloramphenicol, which is a specific inhibitor of mitochondrial protein synthesis. It is concluded that germination requires the early synthesis of oxidized nicotinamide adenine dinucleotide and generation of respiratory substrates and one or more mitochondrially synthesized proteins.
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PMID:Respiratory competence of Dictyostelium discoideum spores. 19 71

The isolated head fragment of myosin is a motor protein that is able to use energy liberated from the hydrolysis of adenosine triphosphate to cause sliding movement of actin filaments. Expression of a myosin fragment nearly equivalent to the amino-terminal globular head domain, generally referred to as subfragment 1, has been achieved by transforming the eukaryotic organism Dictyostelium discoideum with a plasmid that carries a 2.6-kilobase fragment of the cloned Dictyostelium myosin heavy chain gene under the control of the Dictyostelium actin-15 promoter. The recombinant fragment of the myosin heavy chain was purified 2400-fold from one of the resulting cell lines and was found to be functional by the following criteria: the myosin head fragment copurified with the essential and regulatory myosin light chains, decorated actin filaments, and displayed actin-activated adenosine triphosphatase activity. In addition, motility assays in vitro showed that the recombinant myosin fragment is capable of supporting sliding movement of actin filaments.
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PMID:Expression and characterization of a functional myosin head fragment in Dictyostelium discoideum. 253 Jun 29

Myosin II, which converts the energy of adenosine triphosphate hydrolysis into the movement of actin filaments, is a hexamer of two heavy chains, two essential light chains, and two regulatory light chains (RLCs). Dictyostelium myosin II is known to be regulated in vitro by phosphorylation of the RLC. Cells in which the wild-type myosin II heavy chain was replaced with a recombinant form that lacks the binding site for RLC carried out cytokinesis and almost normal development, processes known to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.
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PMID:A functional recombinant myosin II lacking a regulatory light chain-binding site. 826 74

WASP and SCAR homologue (WASH) is a recently identified and evolutionarily conserved regulator of actin polymerization. In this paper, we show that WASH coats mature Dictyostelium discoideum lysosomes and is essential for exocytosis of indigestible material. A related process, the expulsion of the lethal endosomal pathogen Cryptococcus neoformans from mammalian macrophages, also uses WASH-coated vesicles, and cells expressing dominant negative WASH mutants inefficiently expel C. neoformans. D. discoideum WASH causes filamentous actin (F-actin) patches to form on lysosomes, leading to the removal of vacuolar adenosine triphosphatase (V-ATPase) and the neutralization of lysosomes to form postlysosomes. Without WASH, no patches or coats are formed, neutral postlysosomes are not seen, and indigestible material such as dextran is not exocytosed. Similar results occur when actin polymerization is blocked with latrunculin. V-ATPases are known to bind avidly to F-actin. Our data imply a new mechanism, actin-mediated sorting, in which WASH and the Arp2/3 complex polymerize actin on vesicles to drive the separation and recycling of proteins such as the V-ATPase.
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PMID:Actin polymerization driven by WASH causes V-ATPase retrieval and vesicle neutralization before exocytosis. 2160 8

WASH causes actin to polymerize on vesicles involved in retrograde traffic and exocytosis. It is found within a regulatory complex, but the physiological roles of the other four members are unknown. Here we present genetic analysis of the subunits' individual functions in Dictyostelium. Mutants in each subunit are completely blocked in exocytosis. All subunits except FAM21 are required to drive actin assembly on lysosomes. Without actin, lysosomes never recycle vacuolar-type H(+)-adenosine triphosphatase (V-ATPase) or neutralize to form postlysosomes. However, in FAM21 knockout lysosomes, WASH generates excessive, dynamic streams of actin. These successfully remove V-ATPase, neutralize, and form huge postlysosomes. The distinction between WASH and FAM21 phenotypes is conserved in human cells. Thus, FAM21 and WASH act at different steps of a cyclical pathway in which FAM21 mediates recycling of the complex back to acidic lysosomes. Recycling is driven by FAM21's interaction with capping protein, which couples the WASH complex to dynamic actin on vesicles.
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PMID:Cyclical action of the WASH complex: FAM21 and capping protein drive WASH recycling, not initial recruitment. 2336 14