Developmental regulation of a dictyostelium gene encoding a protein homologous to mammalian ras protein

Reymond, Christophe; Gomer, Richard H.; Mehdy, Mona C.; Firtel, Richard A.

doi:10.1016/0092-8674(84)90199-5

Cited by 266 publications

(162 citation statements)

References 29 publications

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“…The knock-out of DGAP1 does not seem to be completely equivalent to expression of activated rasD, since no increase in growth rate has been reported for the rasD-Thrl2 mutant [16]. This is not surprising, since rasD is expressed only during development 4-- [20], while DGAP1 is already present during growth. By a similar argument, DGAP1 does not seem to have the same specificity for members of the ras superfamily as aimless ras-GEF [1].…”

Section: Discussionmentioning

confidence: 95%

DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum

Faix

Dittrich

1996

FEBS Letters

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Section: Discussionmentioning

confidence: 95%

DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum

Faix

Dittrich

1996

FEBS Letters

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“…The response of the enzyme to added RAS2 proteins bound with various guanine nucleotides and their analogs suggests that RAS2 proteins are active in their GTP-bound form and are virtually inactive in their GDP-bound form. Also, active RAS2 protein is not inhibited by inactive RAS2, suggesting that the inactive form does not compete with the active form in binding to its effector.ras genes are ubiquitous in eucaryotes (9,24,27,32). In mammals, they comprise a family of at least three members (H-, K-, and N-ras) which share structural and functional properties.…”

mentioning

confidence: 99%

“…ras genes are ubiquitous in eucaryotes (9,24,27,32). In mammals, they comprise a family of at least three members (H-, K-, and N-ras) which share structural and functional properties.…”

mentioning

confidence: 99%

Guanine nucleotide activation of, and competition between, RAS proteins from Saccharomyces cerevisiae.

Field¹,

Broek²,

Kataoka³

et al. 1987

Mol. Cell. Biol.

111

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In the yeast Saccharomyces cerevisiae, yeast RAS proteins are potent activators of adenylate cyclase. In the present work we measured the activity of adenylate cyclase in membranes from Saccharomyces cerevisiae which overexpress this enzyme. The response of the enzyme to added RAS2 proteins bound with various guanine nucleotides and their analogs suggests that RAS2 proteins are active in their GTP-bound form and are virtually inactive in their GDP-bound form. Also, active RAS2 protein is not inhibited by inactive RAS2, suggesting that the inactive form does not compete with the active form in binding to its effector.ras genes are ubiquitous in eucaryotes (9,24,27,32). In mammals, they comprise a family of at least three members (H-, K-, and N-ras) which share structural and functional properties. They were first identified, in their mutant forms, as potent oncogenes (4,5,7,12,22,26,29,33,36,38,39). Although the normal ras genes are not oncogenic, they too can cause the malignant transformation of cells when expressed at abnormally high levels (7). In mammals, Ras proteins are 21,000-dalton molecules that are localized to the cytoplasmic side of the cell membrane (44). They bind GTP and GDP (30) and have an intrinsic GTPase activity (14,21,35). Moreover, some oncogenic forms of Ras protein are deficient in GTPase activity (14,21,35). Based on these properties, and reasoning by analogy to other known guanine nucleotide-binding proteins, the G proteins (reviewed in reference 15), most investigators think that Ras proteins act as transducers to convey extracellular signals to an intracellular effector pathway. According to this model, Ras protein bound to GTP activates its effector, and then shuts itself off through its intrinsic GTPase activity. Mutant Ras proteins which are defective in GTPase would thus cause abnormally prolonged stimulation of the effector system, explaining their oncogenicity.The RAS1 and RAS2 proteins of the yeast Saccharomyces cerevisiae provide an ideal system for testing aspects of this model. They are structurally, biochemically, and functionally similar to the mammalian Ras proteins, and at least one of their effector systems is known (3,9,10,18,24,37,41,42). The yeast RAS genes were originally isolated by using mammalian ras genes as probes to screen libraries of S. cerevisiae genomic DNA. They encode proteins which are highly homologous to the mammalian Ras proteins, particularly at their amino termini (9, 24). They undergo processing events very similar to those of their mammalian counterparts and localize to membrane fractions (8,13,25,31,44). Like the mammalian proteins, they bind guanine nucleotides; they have an intrinsic GTPase activity, and this activity is reduced in the mutant (17), and that has enabled us to create yeast strains which greatly overexpress that enzyme. As a result, we have been able to develop a more sensitive biochemical assay for Ras proteins. Using this system we have reexamined the guanine nucleotide dependence of RAS2 protein and conclude that RAS2 may b...

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“…Some vertebrales and invertebrates ha ve been shown to contain in their genome a variety of genes, called proto-oncogenes (Barnekow and Schart), 1984;Schartl and Barnekow, 1982;DeFeo-Jones et al, 1983;Bishop, 1985a;Reymond et al, 1984;Goddard et al, 1986). Thesegenes have raised a great interest because it is known that upon integration into the genome of certain avian and mammalian retroviruses they acquired the ability to rapidly cause tumors and to transform cells of the host organisms in vitro.…”

Section: Introducllonmentioning

confidence: 99%

Comparative studies on the src proto-oncogene and its gene product pp60c-src in normal and neoplastic tissues of lower vertebrates

Barnekow

Schartl

1987

Comparative Biochemistry and Physiology Part B: Comparative Bio

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Abstract-!. Oncogenes appear to play an important role in the physiology of transformedas weil as of normal cells.2. Tbe src oncogene is by far the most investigated oncogene in birds and mam~als wit~ respect t.o the biochemical characteristics of its tyrosine kinase activity, although the specd1c functton of thts enzymatic activity still remains to be uncovered.3. Systematic sturlies on the src related kinase activity in lower animals are lacking.4. To contribute to a better understanding of the function of the c-src gene, we performed a comparative study on lower chordates.

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Developmental regulation of a dictyostelium gene encoding a protein homologous to mammalian ras protein

Cited by 266 publications

References 29 publications

DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum

DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum

Guanine nucleotide activation of, and competition between, RAS proteins from Saccharomyces cerevisiae.

Comparative studies on the src proto-oncogene and its gene product pp60c-src in normal and neoplastic tissues of lower vertebrates

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