The PLC1 encoded phospholipase C in the yeast Saccharomyces cerevisiae is essential for glucose-induced phosphatidylinositol turnover and activation of plasma membrane H+-ATPase (Q27936921)

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English	The PLC1 encoded phospholipase C in the yeast Saccharomyces cerevisiae is essential for glucose-induced phosphatidylinositol turnover and activation of plasma membrane H+-ATPase	scientific article

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scholarly article

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PubMed publication ID

1 December 2016

The PLC1 encoded phospholipase C in the yeast Saccharomyces cerevisiae is essential for glucose-induced phosphatidylinositol turnover and activation of plasma membrane H+-ATPase (English)

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PubMed publication ID

1 December 2016

Saccharomyces cerevisiae

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Phosphatidylinositol phospholipase C YPL268W

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GOA release 2020-03-11

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ORCID Public Data File 2021

author name string

P Coccetti

1

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R Tisi

2

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E Martegani

3

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L Souza Teixeira

4

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R Lopes Brandão

5

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I de Miranda Castro

6

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J M Thevelein

7

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language of work or name

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publication date

21 October 1998

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Biochimica et Biophysica Acta

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PubMed publication ID

1 December 2016

1405

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1-3

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147-54

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Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae

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A mutation in PLC1, a candidate phosphoinositide-specific phospholipase C gene from Saccharomyces cerevisiae, causes aberrant mitotic chromosome segregation

1 reference

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The putative phosphoinositide-specific phospholipase C gene, PLC1, of the yeast Saccharomyces cerevisiae is important for cell growth

1 reference

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Essential role for phosphatidylinositol 4,5-bisphosphate in yeast cell proliferation

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Inositol trisphosphate and diacylglycerol: two interacting second messengers

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The response of diphosphoinositide and triphosphoinostitide to perturbations of the adenylate energy charge in cells of Saccharomyces cerevisiae.

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Possible involvement of RAS-encoded proteins in glucose-induced inositolphospholipid turnover in Saccharomyces cerevisiae

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The glucose-induced polyphosphoinositides turnover in Saccharomyces cerevisiae is not dependent on the CDC25-RAS mediated signal transduction pathway

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CDC25-dependent induction of inositol 1,4,5-trisphosphate and diacylglycerol in Saccharomyces cerevisiae by nitrogen

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Signal transduction in yeast.

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Eclosion hormone activates phosphatidylinositol hydrolysis in silkworm abdominal ganglia during adult metamorphosis

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Possible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane H(+)-ATPase and cellular proton extrusion in the yeast Saccharomyces cerevisiae

1 reference

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In vivo glucose activation of the yeast plasma membrane ATPase

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Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport

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Analysis of the regulatory domain of yeast plasma membrane H+-ATPase by directed mutagenesis and intragenic suppression

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Glucose-induced activation of plasma membrane H(+)-ATPase in mutants of the yeast Saccharomyces cerevisiae affected in cAMP metabolism, cAMP-dependent protein phosphorylation and the initiation of glycolysis

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Dependence of the kinetics of secondary active transports in yeast on H(+)-ATPase acidification

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High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier

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Polyphosphoinositide breakdown and subsequent exocytosis in the Ca2+/ionophore-induced acrosome reaction of mammalian spermatozoa

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A pathway in the yeast cell division cycle linking protein kinase C (Pkc1) to activation of Cdc28 at START.

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Compound 48/80 is a potent inhibitor of phospholipase C and a dual modulator of phospholipase A2 from human platelet

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Activation of bovine rod outer segment phosphatidylinositol-4,5-bisphosphate phospholipase C by calmodulin antagonists does not depend on calmodulin

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Glucose-independent inhibition of yeast plasma-membrane H+-ATPase by calmodulin antagonists

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Constitutive glucose-induced activation of the Ras-cAMP pathway and aberrant stationary-phase entry on a glucose-containing medium in the Saccharomyces cerevisiae glucose-repression mutant hex2

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Identifiers

10.1016/S0167-4889(98)00099-8

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PubMed publication ID

1 reference

PubMed publication ID

1 December 2016

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